{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,14]],"date-time":"2026-06-14T15:47:16Z","timestamp":1781452036913,"version":"3.54.1"},"reference-count":121,"publisher":"Walter de Gruyter GmbH","issue":"1","license":[{"start":{"date-parts":[[2020,1,1]],"date-time":"2020-01-01T00:00:00Z","timestamp":1577836800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,3,17]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The inefficiency of cyanide\/HCN (CN) binding with heme proteins (under physiological regimes) is demonstrated with an assessment of thermodynamics, kinetics, and inhibition constants. The acute onset of toxicity and CN\u2019s mg\/Kg LD\n                    <jats:sub>50<\/jats:sub>\n                    (\u03bcM lethal concentration) suggests that the classical hemeFe binding-based inhibition rationale is untenable to account for the toxicity of CN. In vitro mechanistic probing of CN-mediated inhibition of hemeFe reductionist systems was explored as a murburn model for mitochondrial oxidative phosphorylation (mOxPhos). The effect of CN in haloperoxidase catalyzed chlorine moiety transfer to small organics was considered as an analogous probe for phosphate group transfer in mOxPhos. Similarly, inclusion of CN in peroxidase-catalase mediated one-electron oxidation of small organics was used to explore electron transfer outcomes in mOxPhos, leading to water formation. The free energy correlations from a Hammett study and IC\n                    <jats:sub>50<\/jats:sub>\n                    \/Hill slopes analyses and comparison with ligands\n                    <jats:inline-formula>\n                      <jats:alternatives>\n                        <jats:inline-graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"graphic\/j_bmc-2020-0004_eq_001.png\"\/>\n                        <m:math xmlns:m=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                          <m:mrow>\n                            <m:mrow>\n                              <m:mo>(<\/m:mo>\n                              <m:mrow>\n                                <m:mrow>\n                                  <m:mrow>\n                                    <m:mtext>CO<\/m:mtext>\n                                  <\/m:mrow>\n                                  <m:mo>\/<\/m:mo>\n                                  <m:mrow>\n                                    <m:mrow>\n                                      <m:mrow>\n                                        <m:msub>\n                                          <m:mtext>H<\/m:mtext>\n                                          <m:mn>2<\/m:mn>\n                                        <\/m:msub>\n                                        <m:mtext>S<\/m:mtext>\n                                      <\/m:mrow>\n                                      <m:mo>\/<\/m:mo>\n                                      <m:mrow>\n                                        <m:msubsup>\n                                          <m:mtext>N<\/m:mtext>\n                                          <m:mn>3<\/m:mn>\n                                          <m:mtext>-<\/m:mtext>\n                                        <\/m:msubsup>\n                                      <\/m:mrow>\n                                    <\/m:mrow>\n                                  <\/m:mrow>\n                                <\/m:mrow>\n                              <\/m:mrow>\n                              <m:mo>)<\/m:mo>\n                            <\/m:mrow>\n                          <\/m:mrow>\n                        <\/m:math>\n                        <jats:tex-math>$\\left( {\\text{CO}}\/{{{{\\text{H}}_{2}}\\text{S}}\/{\\text{N}_{3}^{\\text{-}}}\\;}\\; \\right)$<\/jats:tex-math>\n                      <\/jats:alternatives>\n                    <\/jats:inline-formula>\n                    provide insights into the involvement of diffusible radicals and proton-equilibriums, explaining analogous outcomes in mOxPhos chemistry. Further, we demonstrate that superoxide (diffusible reactive oxygen species, DROS) enables in vitro ATP synthesis from ADP+phosphate, and show that this reaction is inhibited by CN. Therefore, practically instantaneous CN ion-radical interactions with DROS in matrix catalytically disrupt mOxPhos, explaining the acute lethal effect of CN.\n                  <\/jats:p>","DOI":"10.1515\/bmc-2020-0004","type":"journal-article","created":{"date-parts":[[2020,3,18]],"date-time":"2020-03-18T09:33:30Z","timestamp":1584524010000},"page":"32-56","source":"Crossref","is-referenced-by-count":38,"title":["Acute toxicity of cyanide in aerobic respiration: Theoretical and experimental support for murburn explanation"],"prefix":"10.1515","volume":"11","author":[{"given":"Kelath Murali","family":"Manoj","sequence":"first","affiliation":[{"name":"Satyamjayatu: The Science & Ethics Foundation Snehatheeram , Kulappully, Shoranur-2 (PO) , Kerala , India -679122"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Surjith","family":"Ramasamy","sequence":"additional","affiliation":[{"name":"Department of Biosciences and Bioengineering , Indian Institute of Technology Guwahati , Guwahati , Assam , India -781039"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abhinav","family":"Parashar","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Vignan\u2019s Foundation for Science, Technology & Research , Vadlamudi , Guntur , India -522213"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel Andrew","family":"Gideon","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Bishop Heber College , Tiruchirappalli , Tamil Nadu , India -620017"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vidhu","family":"Soman","sequence":"additional","affiliation":[{"name":"Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi , New Delhi , India -110016"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vivian David","family":"Jacob","sequence":"additional","affiliation":[{"name":"Satyamjayatu: The Science & Ethics Foundation Snehatheeram , Kulappully, Shoranur-2 (PO) , Kerala , India -679122"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kannan","family":"Pakshirajan","sequence":"additional","affiliation":[{"name":"Department of Biosciences and Bioengineering , Indian Institute of Technology Guwahati , Guwahati , Assam , India -781039"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2020,3,17]]},"reference":[{"key":"2025120518330407317_j_bmc-2020-0004_ref_001_w2aab3b7c13b1b6b1ab2b2b1Aa","doi-asserted-by":"crossref","unstructured":"Musshoff F, Schmidt P, Daldrup T, Madea B. Cyanide fatalities: case studies of four suicides and one homicide. Am J Forensic Med Pathol. 2002 Dec;23(4):315\u201320.","DOI":"10.1097\/00000433-200212000-00002"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_002_w2aab3b7c13b1b6b1ab2b2b2Aa","unstructured":"Alberts B, Bray D, Lewis J, Raff M, Roberts K, Watson JD. Molecular Biology of the Cell. 3rd ed. New York: Garland Science; 1994."},{"key":"2025120518330407317_j_bmc-2020-0004_ref_003_w2aab3b7c13b1b6b1ab2b2b3Aa","doi-asserted-by":"crossref","unstructured":"Parashar A, Venkatachalam A, Gideon DA, Manoj KM. Cyanide does more to inhibit heme enzymes, than merely serving as an active-site ligand. Biochem Biophys Res Commun. 2014 Dec;455(3-4):190\u20133.","DOI":"10.1016\/j.bbrc.2014.10.137"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_004_w2aab3b7c13b1b6b1ab2b2b4Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Parashar A, Venkatachalam A, Goyal S, Satyalipsu, Singh PG, et al. Atypical profiles and modulations of heme-enzymes catalyzed outcomes by low amounts of diverse additives suggest diffusible radicals\u2019 obligatory involvement in such redox reactions. Biochimie. 2016 Jun;125:91\u2013111.","DOI":"10.1016\/j.biochi.2016.03.003"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_005_w2aab3b7c13b1b6b1ab2b2b5Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Gade SK, Venkatachalam A, Gideon DA. Electron transfer amongst flavo- and hemo-proteins: diffusible species effect the relay processes, not protein\u2013protein binding. RSC Advances. 2016;6(29):24121\u20139.","DOI":"10.1039\/C5RA26122H"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_006_w2aab3b7c13b1b6b1ab2b2b6Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Baburaj A, Ephraim B, Pappachan F, Maviliparambathu PP, Vijayan UK, et al. Explaining the atypical reaction profiles of heme enzymes with a novel mechanistic hypothesis and kinetic treatment. PLoS One. 2010 May;5(5):e10601.","DOI":"10.1371\/journal.pone.0010601"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_007_w2aab3b7c13b1b6b1ab2b2b7Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Gade SK, Mathew L. Cytochrome P450 reductase: a harbinger of diffusible reduced oxygen species. PLoS One. 2010 Oct;5(10):e13272.","DOI":"10.1371\/journal.pone.0013272"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_008_w2aab3b7c13b1b6b1ab2b2b8Aa","doi-asserted-by":"crossref","unstructured":"Gideon DA, Kumari R, Lynn AM, Manoj KM. What is the functional role of N-terminal transmembrane helices in the metabolism mediated by liver microsomal cytochrome P450 and its reductase? Cell Biochem Biophys. 2012 Feb;63(1):35\u201345.","DOI":"10.1007\/s12013-012-9339-0"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_009_w2aab3b7c13b1b6b1ab2b2b9Aa","doi-asserted-by":"crossref","unstructured":"Parashar A, Gade SK, Potnuru M, Madhavan N, Manoj KM. The curious case of benzbromarone: insight into super-inhibition of cytochrome P450. PLoS One. 2014 Mar;9(3):e89967.","DOI":"10.1371\/journal.pone.0089967"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_010_w2aab3b7c13b1b6b1ab2b2c10Aa","doi-asserted-by":"crossref","unstructured":"Venkatachalam A, Parashar A, Manoj KM. Functioning of drug-metabolizing microsomal cytochrome P450s: in silico probing of proteins suggests that the distal heme \u2018active site\u2019 pocket plays a relatively \u2018passive role\u2019 in some enzyme-substrate interactions. In Silico Pharmacol. 2016 Dec;4(1):2.","DOI":"10.1186\/s40203-016-0016-7"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_011_w2aab3b7c13b1b6b1ab2b2c11Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Parashar A, Gade SK, Venkatachalam A. Functioning of microsomal cytochrome P450s: murburn concept explains the metabolism of xenobiotics in hepatocytes. Front Pharmacol. 2016 Jun;7:161.","DOI":"10.3389\/fphar.2016.00161"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_012_w2aab3b7c13b1b6b1ab2b2c12Aa","doi-asserted-by":"crossref","unstructured":"Parashar A, Gideon DA, Manoj KM. Murburn concept: a molecular explanation for hormetic and idiosyncratic dose responses. Dose Response. 2018 May;16(2):1559325818774421.","DOI":"10.1177\/1559325818774421"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_013_w2aab3b7c13b1b6b1ab2b2c13Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM. Debunking chemiosmosis and proposing murburn concept as the operative principle for cellular respiration. Biomed Rev. 2018 Mar;28(0):31\u201348.","DOI":"10.14748\/bmr.v28.4450"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_014_w2aab3b7c13b1b6b1ab2b2c14Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM. Aerobic Respiration: criticism of the proton-centric explanation involving rotary adenosine triphosphate synthesis, chemiosmosis principle, proton pumps and electron transport chain. Biochem Insights. 2018 Dec;11:1178626418818442.","DOI":"10.1177\/1178626418818442"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_015_w2aab3b7c13b1b6b1ab2b2c15Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM. The ubiquitous biochemical logic of murburn concept. Biomed Rev. 2018;29(0):89\u201397.","DOI":"10.14748\/bmr.v29.5854"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_016_w2aab3b7c13b1b6b1ab2b2c16Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Gideon DA, Jacob VD. Murburn scheme for mitochondrial thermogenesis. Biomed Rev. 2018;29(0):73\u201382.","DOI":"10.14748\/bmr.v29.5852"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_017_w2aab3b7c13b1b6b1ab2b2c17Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Parashar A, David Jacob V, Ramasamy S. Aerobic respiration: proof of concept for the oxygen-centric murburn perspective. J Biomol Struct Dyn. 2019 Oct;37(17):4542\u201356.","DOI":"10.1080\/07391102.2018.1552896"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_018_w2aab3b7c13b1b6b1ab2b2c18Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Soman V, David Jacob V, Parashar A, Gideon DA, Kumar M, et al. Chemiosmotic and murburn explanations for aerobic respiration: predictive capabilities, structure-function correlations and chemico-physical logic. Arch Biochem Biophys. 2019 Nov;676:108128.","DOI":"10.1016\/j.abb.2019.108128"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_019_w2aab3b7c13b1b6b1ab2b2c19Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM. Refutation of the cation-centric torsional ATP synthesis model and advocating murburn scheme for mitochondrial oxidative phosphorylation. Biophys Chem. 2020 Feb;257:106278.","DOI":"10.1016\/j.bpc.2019.106278"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_020_w2aab3b7c13b1b6b1ab2b2c20Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM. Murburn concept: a paradigm shift in cellular metabolism and physiology. Biomol Concepts. 2020 Jan;11(1):7\u201322.","DOI":"10.1515\/bmc-2020-0002"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_021_w2aab3b7c13b1b6b1ab2b2c21Aa","doi-asserted-by":"crossref","unstructured":"Srinivasan S, Avadhani NG. Cytochrome c oxidase dysfunction in oxidative stress. Free Radic Biol Med. 2012 Sep;53(6):1252\u201363.","DOI":"10.1016\/j.freeradbiomed.2012.07.021"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_022_w2aab3b7c13b1b6b1ab2b2c22Aa","doi-asserted-by":"crossref","unstructured":"Chicherin IV, Dashinimaev E, Baleva M, Krasheninnikov I, Levitskii S, Kamenski P. Cytochrome c oxidase on the crossroads of transcriptional regulation and bioenergetics. Front Physiol. 2019 May;10:644.","DOI":"10.3389\/fphys.2019.00644"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_023_w2aab3b7c13b1b6b1ab2b2c23Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Yi X, Rai GP, Hager LP. A kinetic epoxidation assay for chloroperoxidase. Biochem Biophys Res Commun. 1999 Dec;266(2):301\u20133.","DOI":"10.1006\/bbrc.1999.1810"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_024_w2aab3b7c13b1b6b1ab2b2c24Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Lakner FJ, Hager LP. Epoxidation of indene by chloroperoxidase. J Mol Catal, B Enzym. 2000;9(1):107\u201311.","DOI":"10.1016\/S1381-1177(99)00118-6"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_025_w2aab3b7c13b1b6b1ab2b2c25Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Hager LP. Utilization of peroxide and its relevance in oxygen insertion reactions catalyzed by chloroperoxidase. Biochim Biophys Acta. 2001 Jun;1547(2):408\u201317.","DOI":"10.1016\/S0167-4838(01)00210-2"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_026_w2aab3b7c13b1b6b1ab2b2c26Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Hager LP. A colorimetric method for detection and quantification of chlorinating activity of hemeperoxidases. Anal Biochem. 2006 Jan;348(1):84\u20136.","DOI":"10.1016\/j.ab.2005.10.014"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_027_w2aab3b7c13b1b6b1ab2b2c27Aa","doi-asserted-by":"crossref","unstructured":"Murali Manoj K. Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process. Biochim Biophys Acta. 2006 Aug;1764(8):1325\u201339.","DOI":"10.1016\/j.bbapap.2006.05.012"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_028_w2aab3b7c13b1b6b1ab2b2c28Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Hager LP. Chloroperoxidase, a janus enzyme. Biochemistry. 2008 Mar;47(9):2997\u20133003.","DOI":"10.1021\/bi7022656"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_029_w2aab3b7c13b1b6b1ab2b2c29Aa","doi-asserted-by":"crossref","unstructured":"Andrew D, Hager L, Manoj KM. The intriguing enhancement of chloroperoxidase mediated one-electron oxidations by azide, a known active-site ligand. Biochem Biophys Res Commun. 2011 Dec;415(4):646\u20139.","DOI":"10.1016\/j.bbrc.2011.10.128"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_030_w2aab3b7c13b1b6b1ab2b2c30Aa","doi-asserted-by":"crossref","unstructured":"Parashar A, Manoj KM. Traces of certain drug molecules can enhance heme-enzyme catalytic outcomes. Biochem Biophys Res Commun. 2012 Jan;417(3):1041\u20135.","DOI":"10.1016\/j.bbrc.2011.12.090"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_031_w2aab3b7c13b1b6b1ab2b2c31Aa","doi-asserted-by":"crossref","unstructured":"Gade SK, Bhattacharya S, Manoj KM. Redox active molecules cytochrome c and vitamin C enhance heme-enzyme peroxidations by serving as non-specific agents for redox relay. Biochem Biophys Res Commun. 2012 Mar;419(2):211\u20134.","DOI":"10.1016\/j.bbrc.2012.01.149"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_032_w2aab3b7c13b1b6b1ab2b2c32Aa","unstructured":"Dunford BH. Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology. 2nd ed. New York: John Wiley & Sons; 2010."},{"key":"2025120518330407317_j_bmc-2020-0004_ref_033_w2aab3b7c13b1b6b1ab2b2c33Aa","doi-asserted-by":"crossref","unstructured":"Konstantinov AA. Cytochrome c oxidase: intermediates of the catalytic cycle and their energy-coupled interconversion. FEBS Lett. 2012 Mar;586(5):630\u20139.","DOI":"10.1016\/j.febslet.2011.08.037"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_034_w2aab3b7c13b1b6b1ab2b2c34Aa","doi-asserted-by":"crossref","unstructured":"Poulos TL. Heme enzyme structure and function. Chem Rev. 2014 Apr;114(7):3919\u201362.","DOI":"10.1021\/cr400415k"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_035_w2aab3b7c13b1b6b1ab2b2c35Aa","doi-asserted-by":"crossref","unstructured":"Ortiz de Montellano PR. Cytochrome P450: Structure, Mechanism, and Biochemistry. 3rd edn. Kluwer Academic, New York; 2005.","DOI":"10.1007\/b139087"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_036_w2aab3b7c13b1b6b1ab2b2c36Aa","doi-asserted-by":"crossref","unstructured":"Guengerich FP, Yoshimoto FK. Formation and cleavage of C-C bonds by enzymatic oxidation-reduction reactions. Chem Rev. 2018 Jul;118(14):6573\u2013655.","DOI":"10.1021\/acs.chemrev.8b00031"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_037_w2aab3b7c13b1b6b1ab2b2c37Aa","doi-asserted-by":"crossref","unstructured":"Huang X, Groves JT. Oxygen activation and radical transformations in heme proteins and metalloporphyrins. Chem Rev. 2018 Mar;118(5):2491\u2013553.","DOI":"10.1021\/acs.chemrev.7b00373"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_038_w2aab3b7c13b1b6b1ab2b2c38Aa","doi-asserted-by":"crossref","unstructured":"Holzwarth JF, Meyer F, Pickard M, Dunford HB. Mechanism of azide binding to chloroperoxidase and horseradish peroxidase: use of an iodine laser temperature-jump apparatus. Biochemistry. 1988 Aug;27(17):6628\u201333.","DOI":"10.1021\/bi00417a062"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_039_w2aab3b7c13b1b6b1ab2b2c39Aa","unstructured":"Vlasits J. Functional and mechanistic studies on catalase-peroxidase. Doctoral Thesis at University of Natural Resources and Life Sciences (BOKU), Vienna. 2009."},{"key":"2025120518330407317_j_bmc-2020-0004_ref_040_w2aab3b7c13b1b6b1ab2b2c40Aa","doi-asserted-by":"crossref","unstructured":"Cooper CE, Brown GC. The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: chemical mechanism and physiological significance. J Bioenerg Biomembr. 2008 Oct;40(5):533\u20139.","DOI":"10.1007\/s10863-008-9166-6"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_041_w2aab3b7c13b1b6b1ab2b2c41Aa","unstructured":"Liu H, Jiang Y, Luo Y, Jiang W. A simple and rapid determination of ATP, ADP and AMP concentrations in pericarp tissue of litchi fruit by high performance liquid chromatography. Food Technol Biotechnol. 2006;44(4):531\u20134."},{"key":"2025120518330407317_j_bmc-2020-0004_ref_042_w2aab3b7c13b1b6b1ab2b2c42Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM, Soman V. Classical and murburn explanations for acute toxicity of cyanide in aerobic respiration: A personal perspective. Toxicology. 2020 Jan;432:152369.","DOI":"10.1016\/j.tox.2020.152369"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_043_w2aab3b7c13b1b6b1ab2b2c43Aa","doi-asserted-by":"crossref","unstructured":"Ballas SK. Erythrocyte concentration and volume are inversely related. Clin Chim Acta. 1987 Apr;164(2):243\u20134.","DOI":"10.1016\/0009-8981(87)90078-7"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_044_w2aab3b7c13b1b6b1ab2b2c44Aa","doi-asserted-by":"crossref","unstructured":"D\u2019Alessandro A, Kriebardis AG, Rinalducci S, Antonelou MH, Hansen KC, Papassideri IS, et al. An update on red blood cell storage lesions, as gleaned through biochemistry and omics technologies. Transfusion. 2015 Jan;55(1):205\u201319.","DOI":"10.1111\/trf.12804"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_045_w2aab3b7c13b1b6b1ab2b2c45Aa","doi-asserted-by":"crossref","unstructured":"Anseeuw K, Delvau N, Burillo-Putze G, De Iaco F, Geldner G, Holmstr\u00f6m P, et al. Cyanide poisoning by fire smoke inhalation: a European expert consensus. Eur J Emerg Med. 2013 Feb;20(1):2\u20139.","DOI":"10.1097\/MEJ.0b013e328357170b"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_046_w2aab3b7c13b1b6b1ab2b2c46Aa","doi-asserted-by":"crossref","unstructured":"Schwerzmann K, Cruz-Orive LM, Eggman R, S\u00e4nger A, Weibel ER. Molecular architecture of the inner membrane of mitochondria from rat liver: a combined biochemical and stereological study. J Cell Biol. 1986 Jan;102(1):97\u2013103.","DOI":"10.1083\/jcb.102.1.97"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_047_w2aab3b7c13b1b6b1ab2b2c47Aa","doi-asserted-by":"crossref","unstructured":"Milo R, Phillips R. Cell Biology by the Numbers. New York: Taylor & Francis Group; 2016.","DOI":"10.1201\/9780429258770"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_048_w2aab3b7c13b1b6b1ab2b2c48Aa","doi-asserted-by":"crossref","unstructured":"Bianconi E, Piovesan A, Facchin F, Beraudi A, Casadei R, Frabetti F, et al. An estimation of the number of cells in the human body. Ann Hum Biol. 2013 Nov-Dec;40(6):463\u201371.","DOI":"10.3109\/03014460.2013.807878"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_049_w2aab3b7c13b1b6b1ab2b2c49Aa","doi-asserted-by":"crossref","unstructured":"Hall AH, Saiers J, Baud F. Which cyanide antidote? Crit Rev Toxicol. 2009;39(7):541\u201352.","DOI":"10.1080\/10408440802304944"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_050_w2aab3b7c13b1b6b1ab2b2c50Aa","unstructured":"Evans DA. pKa \u2019s of inorganic and oxo-acids. Harvard University, 2005. http:\/\/evans.rc.fas.harvard.edu\/pdf\/evans_pKa_table.pdf"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_051_w2aab3b7c13b1b6b1ab2b2c51Aa","doi-asserted-by":"crossref","unstructured":"Raza SK, Jaiswal DK. Mechanism of cyanide toxicity and efficacy of its antidotes. Def Sci J. 1994;44(4):331\u201340.","DOI":"10.14429\/dsj.44.4188"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_052_w2aab3b7c13b1b6b1ab2b2c52Aa","unstructured":"Taylor J, Roney N, Harper C, Fransen ME, Swarts S. Toxicological Profile for Cyanide. Agency for Toxic Substances and Disease Registry (US). 2006. https:\/\/www.atsdr.cdc.gov\/toxprofiles\/tp8.pdf"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_053_w2aab3b7c13b1b6b1ab2b2c53Aa","doi-asserted-by":"crossref","unstructured":"Antonini E, Brunori M, Greenwood C, Malmstr\u00f6m BG, Rotilio GC. The interaction of cyanide with cytochrome oxidase. Eur J Biochem. 1971 Nov;23(2):396\u2370400.","DOI":"10.1111\/j.1432-1033.1971.tb01633.x"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_054_w2aab3b7c13b1b6b1ab2b2c54Aa","doi-asserted-by":"crossref","unstructured":"Cuvelier ME, Soto P, Courtois F, Broyart B, Bonazzi C. Oxygen solubility measured in aqueous or oily media by a method using a non-invasive sensor. Food Control. 2017;73:1466\u201373.","DOI":"10.1016\/j.foodcont.2016.11.008"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_055_w2aab3b7c13b1b6b1ab2b2c55Aa","doi-asserted-by":"crossref","unstructured":"Jones MG, Bickar D, Wilson MT, Brunori M, Colosimo A, Sarti P. A re-examination of the reactions of cyanide with cytochrome c oxidase. Biochem J. 1984 May;220(1):57\u201366.","DOI":"10.1042\/bj2200057"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_056_w2aab3b7c13b1b6b1ab2b2c56Aa","doi-asserted-by":"crossref","unstructured":"Bienfait HF, Jacobs JM, Slater EC. Mitochondrial oxygen affinity as a function of redox and phosphate potentials. Biochim Biophys Acta. 1975 Mar;376(3):446\u201357.","DOI":"10.1016\/0005-2728(75)90166-8"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_057_w2aab3b7c13b1b6b1ab2b2c57Aa","doi-asserted-by":"crossref","unstructured":"Verkhovsky MI, Morgan JE, Wikstr\u00f6m M. Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase. Biochemistry. 1994 Mar;33(10):3079\u2013 86.","DOI":"10.1021\/bi00176a042"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_058_w2aab3b7c13b1b6b1ab2b2c58Aa","doi-asserted-by":"crossref","unstructured":"Li J, Noll BC, Schulz CE, Scheidt WR. Comparison of cyanide and carbon monoxide as ligands in iron(II) porphyrinates. Angew Chem Int Ed Engl. 2009;48(27):5010\u20133.","DOI":"10.1002\/anie.200901434"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_059_w2aab3b7c13b1b6b1ab2b2c59Aa","doi-asserted-by":"crossref","unstructured":"Petersen LC. The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase. Biochim Biophys Acta. 1977 May;460(2):299\u2013307.","DOI":"10.1016\/0005-2728(77)90216-X"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_060_w2aab3b7c13b1b6b1ab2b2c60Aa","doi-asserted-by":"crossref","unstructured":"Hansen FB, Nicholls P. Control of respiration in proteoliposomes containing cytochrome aa3. II. Inhibition by carbon monoxide and azide. Biochim Biophys Acta. 1978 Jun;502(3):400\u20138.","DOI":"10.1016\/0005-2728(78)90073-7"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_061_w2aab3b7c13b1b6b1ab2b2c61Aa","unstructured":"National Research Council. Acute Exposure Guideline Levels for Selected Airborne Chemicals: Volume 8. Washington, DC: The National Academies Press; 2010. https:\/\/www.nap.edu\/catalog\/12770\/acute-exposure-guideline-levels-for-selected-airborne-chemicals-volume-8"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_062_w2aab3b7c13b1b6b1ab2b2c62Aa","doi-asserted-by":"crossref","unstructured":"Wharton DC, Gibson QH. Cytochrome oxidase from Pseudomonas aeruginosa. IV. Reaction with oxygen and carbon monoxide. Biochim Biophys Acta. 1976 Jun;430(3):445\u201353.","DOI":"10.1016\/0005-2728(76)90020-7"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_063_w2aab3b7c13b1b6b1ab2b2c63Aa","doi-asserted-by":"crossref","unstructured":"Leavesley HB, Li L, Prabhakaran K, Borowitz JL, Isom GE. Interaction of cyanide and nitric oxide with cytochrome c oxidase: implications for acute cyanide toxicity. Toxicol Sci. 2008 Jan;101(1):101\u201311.","DOI":"10.1093\/toxsci\/kfm254"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_064_w2aab3b7c13b1b6b1ab2b2c64Aa","doi-asserted-by":"crossref","unstructured":"Geigert J, Neidleman SL, Dalietos DJ, Dewitt SK. Haloperoxidases: enzymatic synthesis of alpha,beta-halohydrins from gaseous alkenes. Appl Environ Microbiol. 1983 Feb;45(2):366\u201374.","DOI":"10.1128\/aem.45.2.366-374.1983"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_065_w2aab3b7c13b1b6b1ab2b2c65Aa","doi-asserted-by":"crossref","unstructured":"Geigert J, Neidleman SL, Dalietos DJ, Dewitt SK. Novel haloperoxidase reaction: synthesis of dihalogenated products. Appl Environ Microbiol. 1983 May;45(5):1575\u201381.","DOI":"10.1128\/aem.45.5.1575-1581.1983"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_066_w2aab3b7c13b1b6b1ab2b2c66Aa","doi-asserted-by":"crossref","unstructured":"Kolar JJ, Lindgren B, Lawesson SO, Nishida T, Enzell CR, Berg JE. Oxidation of styrene by chlorine dioxide and by chlorite in aqueous solutions. Acta Chem Scand A. 1982;36:599\u2013605.","DOI":"10.3891\/acta.chem.scand.36b-0599"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_067_w2aab3b7c13b1b6b1ab2b2c67Aa","doi-asserted-by":"crossref","unstructured":"Silverstein RM, Hager LP. The chloroperoxidase-catalyzed oxidation of thiols and disulfides to sulfenyl chlorides. Biochemistry. 1974 Dec;13(25):5069\u201373.","DOI":"10.1021\/bi00722a001"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_068_w2aab3b7c13b1b6b1ab2b2c68Aa","doi-asserted-by":"crossref","unstructured":"Libby RD, Thomas JA, Kaiser LW, Hager LP. Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates. J Biol Chem. 1982 May;257(9):5030\u20137.","DOI":"10.1016\/S0021-9258(18)34630-1"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_069_w2aab3b7c13b1b6b1ab2b2c69Aa","doi-asserted-by":"crossref","unstructured":"Ramakrishnan K, Oppenhuizen ME, Saunders S, Fisher J. Stereoselectivity of chloroperoxidase-dependent halogenation. Biochemistry. 1983 Jun;22(13):3271\u20137.","DOI":"10.1021\/bi00282a036"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_070_w2aab3b7c13b1b6b1ab2b2c70Aa","doi-asserted-by":"crossref","unstructured":"Dunford HB, Lambeir AM, Kashem MA, Pickard M. On the mechanism of chlorination by chloroperoxidase. Arch Biochem Biophys. 1987 Jan;252(1):292\u2013302.","DOI":"10.1016\/0003-9861(87)90034-8"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_071_w2aab3b7c13b1b6b1ab2b2c71Aa","doi-asserted-by":"crossref","unstructured":"Wagenknecht HA, Woggon WD. New active-site analogues of chloroperoxidase\u2014syntheses and catalytic reactions. Angew Chem Int Ed Engl. 1997 Mar;36(4):390\u20132.","DOI":"10.1002\/anie.199703901"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_072_w2aab3b7c13b1b6b1ab2b2c72Aa","doi-asserted-by":"crossref","unstructured":"Murphy CD. New frontiers in biological halogenation. J Appl Microbiol. 2003;94(4):539\u201348.","DOI":"10.1046\/j.1365-2672.2003.01900.x"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_073_w2aab3b7c13b1b6b1ab2b2c73Aa","doi-asserted-by":"crossref","unstructured":"Griffin BW. Mechanism of halide-stimulated activity of chloroperoxidase evidence for enzymatic formation of free hypohalous acid. Biochem Biophys Res Commun. 1983 Nov;116(3):873\u20139.","DOI":"10.1016\/S0006-291X(83)80223-X"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_074_w2aab3b7c13b1b6b1ab2b2c74Aa","doi-asserted-by":"crossref","unstructured":"Griffin BW, Haddox R. Chlorination of NADH: similarities of the HOCl-supported and chloroperoxidase-catalyzed reactions. Arch Biochem Biophys. 1985 May;239(1):305\u20139.","DOI":"10.1016\/0003-9861(85)90840-9"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_075_w2aab3b7c13b1b6b1ab2b2c75Aa","doi-asserted-by":"crossref","unstructured":"Stoin U, Shames AI, Malka I, Bar I, Sasson Y. In situ generation of superoxide anion radical in aqueous medium under ambient conditions. ChemPhysChem. 2013 Dec;14(18):4158\u201364.","DOI":"10.1002\/cphc.201300707"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_076_w2aab3b7c13b1b6b1ab2b2c76Aa","doi-asserted-by":"crossref","unstructured":"Khan AU, Gebauer P, Hager LP. Chloroperoxidase generation of singlet Delta molecular oxygen observed directly by spectroscopy in the 1- to 1.6-mum region. Proc Natl Acad Sci USA. 1983 Sep;80(17):5195\u20137.","DOI":"10.1073\/pnas.80.17.5195"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_077_w2aab3b7c13b1b6b1ab2b2c77Aa","doi-asserted-by":"crossref","unstructured":"Griffin BW, Ashley PL. Evidence for a radical mechanism of halogenation of monochlorodimedone catalyzed by chloroperoxidase. Arch Biochem Biophys. 1984 Aug;233(1):188\u201396.","DOI":"10.1016\/0003-9861(84)90616-7"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_078_w2aab3b7c13b1b6b1ab2b2c78Aa","doi-asserted-by":"crossref","unstructured":"Manchester JI, Dinnocenzo JP, Higgins, Jones JP. Higgins, Jones JP. A new mechanistic probe for cytochrome P450: an application of isotope effect profiles. J Am Chem Soc. 1997 May;119(21):5069\u201370.","DOI":"10.1021\/ja9705250"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_079_w2aab3b7c13b1b6b1ab2b2c79Aa","doi-asserted-by":"crossref","unstructured":"Kuss S, Tanner EE, Ordovas-Montanes M, Compton RG. Electrochemical recognition and quantification of cytochrome c expression in Bacillus subtilis and aerobe\/anaerobe Escherichia coli using N,N,N\u2019,N\u2019-tetramethyl-para-phenylene-diamine (TMPD). Chem Sci (Camb). 2017 Nov;8(11):7682\u20138.","DOI":"10.1039\/C7SC03498A"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_080_w2aab3b7c13b1b6b1ab2b2c80Aa","doi-asserted-by":"crossref","unstructured":"Moreno SN, Stolze K, Janzen EG, Mason RP. Oxidation of cyanide to the cyanyl radical by peroxidase\/H2O2 systems as determined by spin trapping. Arch Biochem Biophys. 1988 Sep;265(2):267\u201371.","DOI":"10.1016\/0003-9861(88)90127-0"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_081_w2aab3b7c13b1b6b1ab2b2c81Aa","doi-asserted-by":"crossref","unstructured":"Chen YR, Sturgeon BE, Gunther MR, Mason RP. Electron spin resonance investigation of the cyanyl and azidyl radical formation by cytochrome c oxidase. J Biol Chem. 1999 Aug;274(35):24611\u20136.","DOI":"10.1074\/jbc.274.35.24611"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_082_w2aab3b7c13b1b6b1ab2b2c82Aa","doi-asserted-by":"crossref","unstructured":"Janzen EG, Stronks HJ, Nutter DE Jr, Davis ER, Blount HN, Poyer JL, et al. Jr., Davis, E.R., Blount, H.N., Poyer, J.L., McCay P. Spin trapping azidyl (N3*), cyanatyl (OCN*), cyanyl (*CN) radicals, and chlorine atom (Cl*). Can J Chem. 1980;58(15):1596\u20138.","DOI":"10.1139\/v80-252"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_083_w2aab3b7c13b1b6b1ab2b2c83Aa","doi-asserted-by":"crossref","unstructured":"Sono M, Dawson JH, Hall K, Hager LP. Ligand and halide binding properties of chloroperoxidase: peroxidase-type active site heme environment with cytochrome P-450 type endogenous axial ligand and spectroscopic properties. Biochemistry. 1986 Jan;25(2):347\u201356.","DOI":"10.1021\/bi00350a011"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_084_w2aab3b7c13b1b6b1ab2b2c84Aa","doi-asserted-by":"crossref","unstructured":"Yonetani T, Ray GS. Studies on cytochrome oxidase. VI. Kinetics of the aerobic oxidation of ferrocytochrome c by cytochrome oxidase. J Biol Chem. 1965 Aug;240:3392\u20138.","DOI":"10.1016\/S0021-9258(18)97230-3"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_085_w2aab3b7c13b1b6b1ab2b2c85Aa","doi-asserted-by":"crossref","unstructured":"Wainio WW, Greenless J. Complexes of cytochrome c oxidase with cyanide and carbon monoxide. Arch Biochem Biophys. 1960 Sep;90(1):18\u201321.","DOI":"10.1016\/0003-9861(60)90605-6"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_086_w2aab3b7c13b1b6b1ab2b2c86Aa","unstructured":"Cayman Chemicals. MitoCheck \u00ae Complex IV Activity Assay Kit. 2014;(700990):700930. https:\/\/static.caymanchem.com\/insert\/700990.pdf"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_087_w2aab3b7c13b1b6b1ab2b2c87Aa","doi-asserted-by":"crossref","unstructured":"Myers DK, Slater EC. The enzymic hydrolysis of adenosine triphosphate by liver mitochondria. I. Activities at different pH values. Biochem J. 1957 Dec;67(4):558\u201372.","DOI":"10.1042\/bj0670558"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_088_w2aab3b7c13b1b6b1ab2b2c88Aa","doi-asserted-by":"crossref","unstructured":"Myers DK, Slater EC. The enzymic hydrolysis of adenosine triphosphate by liver mitochondria. 2. Effect of inhibitors and added cofactors. Biochem J. 1957 Dec;67(4):572\u20138.","DOI":"10.1042\/bj0670572"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_089_w2aab3b7c13b1b6b1ab2b2c89Aa","doi-asserted-by":"crossref","unstructured":"Chance B, Conrad H. Acid-linked functions of intermediates in oxidative phosphorylation. II. Experimental studies of the effect of pH upon respiratory, phosphorylative and transfer activities of liver and heart mitochondria. J Biol Chem. 1959 Jun;234(6):1568\u201370.","DOI":"10.1016\/S0021-9258(18)70051-3"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_090_w2aab3b7c13b1b6b1ab2b2c90Aa","doi-asserted-by":"crossref","unstructured":"Mailer K. Superoxide radical as electron donor for oxidative phosphorylation of ADP. Biochem Biophys Res Commun. 1990 Jul;170(1):59\u201364.","DOI":"10.1016\/0006-291X(90)91240-S"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_091_w2aab3b7c13b1b6b1ab2b2c91Aa","doi-asserted-by":"crossref","unstructured":"Tyszkiewicz E, Roux E. Role of the Superoxide Anion O 2 - and Hydroxyl Radical (OH-) in ATP Synthesis Obtained with Spinach Chloroplasts in Darkness. Progress in Photosynthesis Research. Dordrecht: Springer Netherlands; 1987. pp. 213\u20136.","DOI":"10.1007\/978-94-017-0516-5_45"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_092_w2aab3b7c13b1b6b1ab2b2c92Aa","doi-asserted-by":"crossref","unstructured":"Pierre JL, Fontecave M. Iron and activated oxygen species in biology: the basic chemistry. Biometals. 1999 Sep;12(3):195\u20139.","DOI":"10.1023\/A:1009252919854"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_093_w2aab3b7c13b1b6b1ab2b2c93Aa","doi-asserted-by":"crossref","unstructured":"Kellogg EW 3rd, Fridovich I. Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system. J Biol Chem. 1975 Nov;250(22):8812\u20137.","DOI":"10.1016\/S0021-9258(19)40745-X"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_094_w2aab3b7c13b1b6b1ab2b2c94Aa","doi-asserted-by":"crossref","unstructured":"Nakano M, Noguchi T, Tsutsumi Y, Sugioka K, Shimizu Y, Tsuji Y, et al. Indirect evidence for superoxide anion and singlet oxygen generated by NADPH\u2014NADPH-dependent cytochrome c reductase and by L-alpha-hydroxyacid\u2014L-amino acid oxidase at high pH. Proc Soc Exp Biol Med. 1974 Oct;147(1):140\u20133.","DOI":"10.3181\/00379727-147-38298"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_095_w2aab3b7c13b1b6b1ab2b2c95Aa","doi-asserted-by":"crossref","unstructured":"Kerver ED, Vogels IM, Bosch KS, Vreeling-Sindel\u00e1rov\u00e1 H, Van den Munckhof RJ, Frederiks WM. In situ detection of spontaneous superoxide anion and singlet oxygen production by mitochondria in rat liver and small intestine. Histochem J. 1997 Mar;29(3):229\u201337.","DOI":"10.1023\/A:1026453926517"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_096_w2aab3b7c13b1b6b1ab2b2c96Aa","doi-asserted-by":"crossref","unstructured":"Chance B. The reaction of catalase and cyanide. J Biol Chem. 1949 Jul;179(3):1299\u2013309.","DOI":"10.1016\/S0021-9258(18)56796-X"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_097_w2aab3b7c13b1b6b1ab2b2c97Aa","doi-asserted-by":"crossref","unstructured":"Chance B. Oxidase and peroxidase reactions in the presence of dihydroxymaleic acid. J Biol Chem. 1952 May;197(2):577\u201389.","DOI":"10.1016\/S0021-9258(18)55612-X"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_098_w2aab3b7c13b1b6b1ab2b2c98Aa","doi-asserted-by":"crossref","unstructured":"Gideon DA, Jacob VD, Manoj KM. 2020: Murburn concept heralds a new era in cellular bioenergetics. Biomedical Reviews. 2019;30:89\u201398.","DOI":"10.14748\/bmr.v30.6390"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_099_w2aab3b7c13b1b6b1ab2b2c99Aa","doi-asserted-by":"crossref","unstructured":"Barr DP, Mason RP. Mechanism of radical production from the reaction of cytochrome c with organic hydroperoxides. An ESR spin trapping investigation. J Biol Chem. 1995 May;270(21):12709\u201316.","DOI":"10.1074\/jbc.270.21.12709"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_100_w2aab3b7c13b1b6b1ab2b2d100Aa","doi-asserted-by":"crossref","unstructured":"Chen YR, Deterding LJ, Tomer KB, Mason RP. Nature of the inhibition of horseradish peroxidase and mitochondrial cytochrome c oxidase by cyanyl radical. Biochemistry. 2000 Apr;39(15):4415\u201322.","DOI":"10.1021\/bi992652+"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_101_w2aab3b7c13b1b6b1ab2b2d101Aa","doi-asserted-by":"crossref","unstructured":"Delporte C, Zouaoui Boudjeltia K, Furtm\u00fcller PG, Maki RA, Dieu M, Noyon C, et al. Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: A potential carbamylation route involved in the formation of atherosclerotic plaques? J Biol Chem. 2018 Apr;293(17):6374\u201386.","DOI":"10.1074\/jbc.M117.801076"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_102_w2aab3b7c13b1b6b1ab2b2d102Aa","unstructured":"Boettern L. Carbon monoxide and hydrogen sulfide: the leading toxic hazards in confined space entry. Biosystems Applications Note No. AN2000-2Rev02. 2000;1\u20132. https:\/\/www.brandtinst.com\/biosystems\/appnotes\/Downloads\/3.%20CO-&-H2S_Leading_Toxic_Hazards.pdf"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_103_w2aab3b7c13b1b6b1ab2b2d103Aa","doi-asserted-by":"crossref","unstructured":"Affourtit C, Albury MS, Crichton PG, Moore AL. Exploring the molecular nature of alternative oxidase regulation and catalysis. FEBS Lett. 2002 Jan;510(3):121\u20136.","DOI":"10.1016\/S0014-5793(01)03261-6"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_104_w2aab3b7c13b1b6b1ab2b2d104Aa","unstructured":"Rubright S. Cyanide and hydrogen sulfide: A review of two blood gases, their environmental sources, and potential risks. University of Pittsburgh. http:\/\/d-scholarship.pitt.edu\/30128\/1\/Rubright_ETD_12_2016.pdf"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_105_w2aab3b7c13b1b6b1ab2b2d105Aa","doi-asserted-by":"crossref","unstructured":"Rao P, Singh P, Yadav SK, Gujar NL, Bhattacharya R. Acute toxicity of some synthetic cyanogens in rats: time-dependent cyanide generation and cytochrome oxidase inhibition in soft tissues after sub-lethal oral intoxication. Food Chem Toxicol. 2013 Sep;59:595\u2013609.","DOI":"10.1016\/j.fct.2013.06.035"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_106_w2aab3b7c13b1b6b1ab2b2d106Aa","doi-asserted-by":"crossref","unstructured":"Kimani S, Moterroso V, Morales P, Wagner J, Kipruto S, Bukachi F, et al. Cross-species and tissue variations in cyanide detoxification rates in rodents and non-human primates on protein-restricted diet. Food Chem Toxicol. 2014 Apr;66:203\u20139.","DOI":"10.1016\/j.fct.2014.01.047"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_107_w2aab3b7c13b1b6b1ab2b2d107Aa","doi-asserted-by":"crossref","unstructured":"Rice NC, Rauscher NA, Langston JL, Myers TM. Behavioral toxicity of sodium cyanide following oral ingestion in rats: dose-dependent onset, severity, survival, and recovery. Food Chem Toxicol. 2018 Apr;114:145\u201354.","DOI":"10.1016\/j.fct.2018.02.033"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_108_w2aab3b7c13b1b6b1ab2b2d108Aa","doi-asserted-by":"crossref","unstructured":"Cressey P, Reeve J. Metabolism of cyanogenic glycosides: A review. Food Chem Toxicol. 2019 Mar;125:225\u201332.","DOI":"10.1016\/j.fct.2019.01.002"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_109_w2aab3b7c13b1b6b1ab2b2d109Aa","doi-asserted-by":"crossref","unstructured":"Bradbury JH, Cliff J, Denton IC. Uptake of wetting method in Africa to reduce cyanide poisoning and konzo from cassava. Food Chem Toxicol. 2011 Mar;49(3):539\u201342.","DOI":"10.1016\/j.fct.2010.04.049"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_110_w2aab3b7c13b1b6b1ab2b2d110Aa","doi-asserted-by":"crossref","unstructured":"Banea JP, Bradbury JH, Mandombi C, Nahimana D, Denton IC, Kuwa N, et al. Control of konzo by detoxification of cassava flour in three villages in the Democratic Republic of Congo. Food Chem Toxicol. 2013 Oct;60:506\u201313.","DOI":"10.1016\/j.fct.2013.08.012"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_111_w2aab3b7c13b1b6b1ab2b2d111Aa","doi-asserted-by":"crossref","unstructured":"Berg SP, Krogmann DW. Mechanism of KCN inhibition of photosystem I. J Biol Chem. 1975 Dec;250(23):8957\u201362.","DOI":"10.1016\/S0021-9258(19)40678-9"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_112_w2aab3b7c13b1b6b1ab2b2d112Aa","doi-asserted-by":"crossref","unstructured":"Forti G, Gerola P. Inhibition of photosynthesis by azide and cyanide and the role of oxygen in photosynthesis. Plant Physiol. 1977 May;59(5):859\u201362.","DOI":"10.1104\/pp.59.5.859"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_113_w2aab3b7c13b1b6b1ab2b2d113Aa","doi-asserted-by":"crossref","unstructured":"Hill R, Szabo M, ur Rehman A, Vass I, Ralph PJ, Larkum AW. ur Rehman A, Vass I, Ralph PJ, Larkum AWD. Inhibition of photosynthetic CO(2) fixation in the coral Pocillopora damicornis and its relationship to thermal bleaching. J Exp Biol. 2014 Jun;217(Pt 12):2150\u201362.","DOI":"10.1242\/jeb.100578"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_114_w2aab3b7c13b1b6b1ab2b2d114Aa","doi-asserted-by":"crossref","unstructured":"Li J, Burgess BK, Corbin JL. Nitrogenase reactivity: cyanide as substrate and inhibitor. Biochemistry. 1982 Aug;21(18):4393\u2013402.","DOI":"10.1021\/bi00261a031"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_115_w2aab3b7c13b1b6b1ab2b2d115Aa","doi-asserted-by":"crossref","unstructured":"Manoj KM. Oxygenic photosynthesis: critiquing the standing explanations and proposing explorative solutions based in murburn concept. OSF Preprints. 2019. doi:10.31219\/osf.io\/3mzfp.","DOI":"10.31219\/osf.io\/3mzfp"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_116_w2aab3b7c13b1b6b1ab2b2d116Aa","doi-asserted-by":"crossref","unstructured":"Gibson QH, Greenwood C. Reactions of cytochrome oxidase with oxygen and carbon monoxide. Biochem J. 1963 Mar;86(3):541\u201354.","DOI":"10.1042\/bj0860541"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_117_w2aab3b7c13b1b6b1ab2b2d117Aa","doi-asserted-by":"crossref","unstructured":"Gibson QH, Palmer G, Wharton DC. The binding of carbon monoxide by cytochrome c oxidase and the ratio of the cytochromes a and a3 J Biol Chem. 1965 Feb;240:915\u201320.","DOI":"10.1016\/S0021-9258(17)45261-6"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_118_w2aab3b7c13b1b6b1ab2b2d118Aa","doi-asserted-by":"crossref","unstructured":"Marshall D, Nicholls P, Wilson M, Cooper C. A comparison of nitric oxide and hydrogen sulphide interactions with mitochondrial cytochrome c oxidase. Nitric Oxide. 2012;27:S11\u20132.","DOI":"10.1016\/j.niox.2012.04.043"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_119_w2aab3b7c13b1b6b1ab2b2d119Aa","doi-asserted-by":"crossref","unstructured":"Li W, Palmer G. Spectroscopic characterization of the interaction of azide and thiocyanate with the binuclear center of cytochrome oxidase: evidence for multiple ligand sites. Biochemistry. 1993 Feb;32(7):1833\u201343.","DOI":"10.1021\/bi00058a018"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_120_w2aab3b7c13b1b6b1ab2b2d120Aa","doi-asserted-by":"crossref","unstructured":"Stannard JN, Horecker BL. The in vitro inhibition of cytochrome oxidase by azide and cyanide. J Biol Chem. 1948 Feb;172(2):599\u2013608.","DOI":"10.1016\/S0021-9258(19)52746-6"},{"key":"2025120518330407317_j_bmc-2020-0004_ref_121_w2aab3b7c13b1b6b1ab2b2d121Aa","doi-asserted-by":"crossref","unstructured":"Wilson DF, Ereci\u0144ska M. Ligands of cytochrome c oxidase. Methods Enzymol. 1978;53:191\u2013201.","DOI":"10.1016\/S0076-6879(78)53024-3"}],"container-title":["Biomolecular Concepts"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.degruyter.com\/view\/journals\/bmc\/11\/1\/article-p32.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/bmc-2020-0004\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/bmc-2020-0004\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,12,5]],"date-time":"2025-12-05T19:05:37Z","timestamp":1764961537000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/bmc-2020-0004\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,1,1]]},"references-count":121,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2020,3,17]]},"published-print":{"date-parts":[[2020,3,17]]}},"alternative-id":["10.1515\/bmc-2020-0004"],"URL":"https:\/\/doi.org\/10.1515\/bmc-2020-0004","relation":{},"ISSN":["1868-503X","1868-5021"],"issn-type":[{"value":"1868-503X","type":"electronic"},{"value":"1868-5021","type":"print"}],"subject":[],"published":{"date-parts":[[2020,1,1]]}}}