{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T11:27:33Z","timestamp":1784287653900,"version":"3.55.0"},"reference-count":89,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,13]],"date-time":"2025-12-13T00:00:00Z","timestamp":1765584000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P20-GM113132"],"award-info":[{"award-number":["P20-GM113132"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01-GM098502"],"award-info":[{"award-number":["R01-GM098502"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Inorganic Biochemistry"],"published-print":{"date-parts":[[2026,3]]},"DOI":"10.1016\/j.jinorgbio.2025.113182","type":"journal-article","created":{"date-parts":[[2025,12,9]],"date-time":"2025-12-09T16:12:09Z","timestamp":1765296729000},"page":"113182","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes"],"prefix":"10.1016","volume":"276","author":[{"given":"Dong-Woo","family":"Shin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fangfang","family":"Zhong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ekaterina V.","family":"Pletneva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"2","key":"10.1016\/j.jinorgbio.2025.113182_bb0005","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.cbpa.2004.02.009","article-title":"Cytochrome c folding dynamics","volume":"8","author":"Winkler","year":"2004","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0010","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.jmb.2004.08.005","article-title":"How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization","volume":"343","author":"Maity","year":"2004","journal-title":"J. Mol. Biol."},{"issue":"14","key":"10.1016\/j.jinorgbio.2025.113182_bb0015","doi-asserted-by":"crossref","first-page":"3809","DOI":"10.1073\/pnas.1522674113","article-title":"Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway","volume":"113","author":"Hu","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"7\u20138","key":"10.1016\/j.jinorgbio.2025.113182_bb0020","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1016\/j.ccr.2010.09.014","article-title":"Protein dynamics and function: making new strides with an old warhorse, the alkaline conformational transition of cytochrome c","volume":"255","author":"Cherney","year":"2011","journal-title":"Coord. Chem. Rev."},{"issue":"1\u20132","key":"10.1016\/j.jinorgbio.2025.113182_bb0025","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0005-2728(98)00109-1","article-title":"Mitochondrial control of apoptosis: the role of cytochrome c","volume":"1366","author":"Cai","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0030","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.abb.2003.12.002","article-title":"The cardiolipin-cytochrome c interaction and the mitochondrial regulation of apoptosis","volume":"423","author":"Iverson","year":"2004","journal-title":"Arch. Biochem. Biophys."},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.113182_bb0035","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1038\/nchembio727","article-title":"Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors","volume":"1","author":"Kagan","year":"2005","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0040","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.jinorgbio.2015.12.025","article-title":"Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability","volume":"158","author":"Goldes","year":"2016","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0045","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2019.110924","article-title":"Comparison of the structural dynamic and mitochondrial electron-transfer properties of the proapoptotic human cytochrome c variants, G41S, Y48H and A51V","volume":"203","author":"Deacon","year":"2020","journal-title":"J. Inorg. Biochem."},{"issue":"23","key":"10.1016\/j.jinorgbio.2025.113182_bb0050","doi-asserted-by":"crossref","first-page":"2950","DOI":"10.1021\/acs.biochem.6b01187","article-title":"Remote perturbations in tertiary contacts trigger ligation of lysine to the heme iron in cytochrome c","volume":"56","author":"Gu","year":"2017","journal-title":"Biochemistry"},{"issue":"20","key":"10.1016\/j.jinorgbio.2025.113182_bb0055","doi-asserted-by":"crossref","first-page":"14085","DOI":"10.1021\/acs.inorgchem.9b02111","article-title":"A heme propionate staples the structure of cytochrome c for methionine ligation to the heme iron","volume":"58","author":"Deng","year":"2019","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0060","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2025.113053","article-title":"Physical and functional effects of substituting coevolved residues from \u03a9-loop C of yeast Iso-1-cytochrome c into human cytochrome c","volume":"274","author":"Frederick","year":"2026","journal-title":"J. Inorg. Biochem."},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.113182_bb0065","doi-asserted-by":"crossref","DOI":"10.3390\/ijms25042163","article-title":"Current understanding of immune thrombocytopenia: a review of pathogenesis and treatment options","volume":"25","author":"Mititelu","year":"2024","journal-title":"Int. J. Mol. Sci."},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.113182_bb0070","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/s00775-024-02044-2","article-title":"Altered conformational dynamics contribute to species-specific effects of cytochrome c mutations on caspase activation","volume":"29","author":"Chin","year":"2024","journal-title":"J. Biol. Inorg. Chem."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0075","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1042\/BJ20130758","article-title":"The hydrogen-peroxide-induced radical behaviour in human cytochrome c\u2013phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant","volume":"456","author":"Rajagopal","year":"2013","journal-title":"Biochem. J."},{"issue":"5","key":"10.1016\/j.jinorgbio.2025.113182_bb0080","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1021\/ja106328k","article-title":"The proapoptotic G41S mutation to human cytochrome c alters the heme electronic structure and increases the electron self-exchange rate","volume":"133","author":"Liptak","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0085","doi-asserted-by":"crossref","DOI":"10.1038\/srep30447","article-title":"Increased dynamics in the 40-57 omega-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation","volume":"6","author":"Karsisiotis","year":"2016","journal-title":"Sci. Rep."},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.113182_bb0090","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/0022-2836(90)90200-6","article-title":"High-resolution three-dimensional structure of horse heart cytochrome c","volume":"214","author":"Bushnell","year":"1990","journal-title":"J. Mol. Biol."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0095","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1007\/s10863-009-9223-9","article-title":"Evolutionary alkaline transition in human cytochrome c","volume":"41","author":"Ying","year":"2009","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0100","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."},{"issue":"13","key":"10.1016\/j.jinorgbio.2025.113182_bb0105","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera--a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0110","doi-asserted-by":"crossref","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"issue":"16","key":"10.1016\/j.jinorgbio.2025.113182_bb0115","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J. Comput. Chem."},{"issue":"13","key":"10.1016\/j.jinorgbio.2025.113182_bb0120","doi-asserted-by":"crossref","first-page":"1613","DOI":"10.1002\/jcc.20079","article-title":"Classical force field parameters for the heme prosthetic group of cytochrome c","volume":"25","author":"Autenrieth","year":"2004","journal-title":"J. Comput. Chem."},{"issue":"11","key":"10.1016\/j.jinorgbio.2025.113182_bb0125","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1002\/jcc.20065","article-title":"Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations","volume":"25","author":"Mackerell","year":"2004","journal-title":"J. Comput. Chem."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0130","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1021\/acs.inorgchem.1c02322","article-title":"Comparing properties of common bioinorganic ligands with switchable variants of cytochrome c","volume":"61","author":"Zhong","year":"2022","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0135","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1-2","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0140","series-title":"Modern Physical Organic Chemistry","author":"Anslyn","year":"2006"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0145","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1073\/pnas.1112312108","article-title":"Conformational properties of cardiolipin-bound cytochrome c","volume":"109","author":"Hanske","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0150","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0003-2697(87)90643-9","article-title":"Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra","volume":"161","author":"Berry","year":"1987","journal-title":"Anal. Biochem."},{"issue":"26","key":"10.1016\/j.jinorgbio.2025.113182_bb0155","doi-asserted-by":"crossref","first-page":"8435","DOI":"10.1021\/jacs.5b01493","article-title":"A compact structure of cytochrome c trapped in a lysine-ligated state: loop refolding and functional implications of a conformational switch","volume":"137","author":"Amacher","year":"2015","journal-title":"J. Am. Chem. Soc."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0160","doi-asserted-by":"crossref","first-page":"E306","DOI":"10.1073\/pnas.1317173111","article-title":"Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins","volume":"111","author":"Zhong","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0165","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/0076-6879(86)31045-0","article-title":"Determination and analysis of urea and guanidine hydrochloride denaturation curves","volume":"131","author":"Pace","year":"1986","journal-title":"Methods Enzymol."},{"issue":"9","key":"10.1016\/j.jinorgbio.2025.113182_bb0170","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1021\/ed083p1325","article-title":"Spectroscopic measurement of the redox potential of cytochrome c for the undergraduate biochemistry laboratory","volume":"83","author":"Craig","year":"2006","journal-title":"J. Chem. Educ."},{"issue":"42","key":"10.1016\/j.jinorgbio.2025.113182_bb0175","doi-asserted-by":"crossref","first-page":"12878","DOI":"10.1021\/jp402104r","article-title":"Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c","volume":"117","author":"Muenzner","year":"2013","journal-title":"J. Phys. Chem. B"},{"issue":"9\u201310","key":"10.1016\/j.jinorgbio.2025.113182_bb0180","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/S0891-5849(98)00315-3","article-title":"Antioxidant activity applying an improved ABTS radical cation decolorization assay","volume":"26","author":"Re","year":"1999","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0185","series-title":"Heme peroxidases","author":"Dunford","year":"1999"},{"issue":"46","key":"10.1016\/j.jinorgbio.2025.113182_bb0190","doi-asserted-by":"crossref","first-page":"6111","DOI":"10.1021\/acs.biochem.7b00890","article-title":"Heightened dynamics of the oxidized Y48H variant of human cytochrome c increases its peroxidatic activity","volume":"56","author":"Deacon","year":"2017","journal-title":"Biochemistry"},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0195","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1042\/BCJ20200793","article-title":"Altered structure and dynamics of pathogenic cytochrome c variants correlate with increased apoptotic activity","volume":"478","author":"Fellner","year":"2021","journal-title":"Biochem. J."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0200","series-title":"Cytochromes c: Evolutionary, Structural and Physicochemical Aspects","author":"Geoffrey","year":"1990"},{"issue":"10","key":"10.1016\/j.jinorgbio.2025.113182_bb0205","doi-asserted-by":"crossref","first-page":"4934","DOI":"10.1016\/S0021-9258(19)69347-6","article-title":"Characterization of conformational heterogeneity in the heme pocket of ferricytochrome c using high field proton nuclear magnetic resonance spectroscopy","volume":"256","author":"Burns","year":"1981","journal-title":"J. Biol. Chem."},{"issue":"44","key":"10.1016\/j.jinorgbio.2025.113182_bb0210","doi-asserted-by":"crossref","first-page":"11234","DOI":"10.1021\/ja971756+","article-title":"Proton-linked protein conformational switching: definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c","volume":"120","author":"Rosell","year":"1998","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0215","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1021\/ja045719b","article-title":"EPR and optical spectroscopic studies of Met80X mutants of yeast ferricytochrome c. models for intermediates in the alkaline transition","volume":"127","author":"Silkstone","year":"2005","journal-title":"J. Am. Chem. Soc."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0220","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1007\/s00775-012-0973-1","article-title":"Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination","volume":"18","author":"Josephs","year":"2013","journal-title":"J. Biol. Inorg. Chem."},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.113182_bb0225","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1039\/B611895J","article-title":"Thermodynamics of protein denatured states","volume":"3","author":"Bowler","year":"2007","journal-title":"Mol. BioSyst."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0230","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.ymeth.2004.03.005","article-title":"Hydrogen exchange methods to study protein folding","volume":"34","author":"Krishna","year":"2004","journal-title":"Methods"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0235","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1560\/PK7U-LEPJ-ETB5-997X","article-title":"Structural models for the alkaline conformers of yeast iso-1-ferricytochrome c","volume":"40","author":"Ness","year":"2000","journal-title":"Isr. J. Chem."},{"issue":"10","key":"10.1016\/j.jinorgbio.2025.113182_bb0240","doi-asserted-by":"crossref","first-page":"2913","DOI":"10.1021\/ja027180s","article-title":"Structural model for an alkaline form of ferricytochrome c","volume":"125","author":"Assfalg","year":"2003","journal-title":"J. Am. Chem. Soc."},{"issue":"10","key":"10.1016\/j.jinorgbio.2025.113182_bb0245","doi-asserted-by":"crossref","first-page":"1873","DOI":"10.1110\/ps.9.10.1873","article-title":"Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange","volume":"9","author":"Mayne","year":"2000","journal-title":"Protein Sci."},{"issue":"15","key":"10.1016\/j.jinorgbio.2025.113182_bb0250","doi-asserted-by":"crossref","first-page":"8312","DOI":"10.1073\/pnas.150239397","article-title":"NMR investigation of ferricytochrome c unfolding: detection of an equilibrium unfolding intermediate and residual structure in the denatured state","volume":"97","author":"Russell","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0255","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1002\/pro.5560060311","article-title":"Fast folding of cytochrome c","volume":"6","author":"Pierce","year":"1997","journal-title":"Protein Sci."},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0260","series-title":"Biological Inorganic Chemistry\u202f: Structure and Reactivity","author":"Bertini","year":"2007"},{"issue":"29","key":"10.1016\/j.jinorgbio.2025.113182_bb0265","doi-asserted-by":"crossref","first-page":"4276","DOI":"10.1021\/acs.biochem.8b00520","article-title":"Naturally occurring disease-related mutations in the 40-57 omega-loop of human cytochrome c control triggering of the alkaline isomerization","volume":"57","author":"Deacon","year":"2018","journal-title":"Biochemistry"},{"issue":"5","key":"10.1016\/j.jinorgbio.2025.113182_bb0270","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.1016\/j.jmb.2006.04.035","article-title":"Order of steps in the cytochrome c folding pathway: evidence for a sequential stabilization mechanism","volume":"359","author":"Krishna","year":"2006","journal-title":"J. Mol. Biol."},{"issue":"26","key":"10.1016\/j.jinorgbio.2025.113182_bb0275","doi-asserted-by":"crossref","first-page":"2921","DOI":"10.1021\/acs.biochem.9b00295","article-title":"Effect of V83G and I81A substitutions to human cytochrome c on acid unfolding and peroxidase activity below a neutral pH","volume":"58","author":"Lei","year":"2019","journal-title":"Biochemistry"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0280","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0005-2795(81)90217-8","article-title":"Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c","volume":"669","author":"Saigo","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"issue":"51","key":"10.1016\/j.jinorgbio.2025.113182_bb0285","doi-asserted-by":"crossref","first-page":"16770","DOI":"10.1021\/jacs.6b10745","article-title":"Cytochrome c can form a well-defined binding pocket for hydrocarbons","volume":"138","author":"McClelland","year":"2016","journal-title":"J. Am. Chem. Soc."},{"issue":"18","key":"10.1016\/j.jinorgbio.2025.113182_bb0290","doi-asserted-by":"crossref","first-page":"6648","DOI":"10.1073\/pnas.1323828111","article-title":"Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity","volume":"111","author":"McClelland","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"25","key":"10.1016\/j.jinorgbio.2025.113182_bb0295","doi-asserted-by":"crossref","first-page":"17542","DOI":"10.1074\/jbc.M710126200","article-title":"Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer","volume":"283","author":"Solmaz","year":"2008","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0300","doi-asserted-by":"crossref","first-page":"291","DOI":"10.15252\/embj.201695021","article-title":"Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode","volume":"36","author":"Shimada","year":"2017","journal-title":"EMBO J."},{"issue":"30","key":"10.1016\/j.jinorgbio.2025.113182_bb0305","doi-asserted-by":"crossref","first-page":"12271","DOI":"10.1073\/pnas.1108320108","article-title":"NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase","volume":"108","author":"Sakamoto","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"5089","key":"10.1016\/j.jinorgbio.2025.113182_bb0310","doi-asserted-by":"crossref","first-page":"1748","DOI":"10.1126\/science.1334573","article-title":"Crystal-structure of a complex between electron-transfer partners, cytochrome-c peroxidase and cytochrome-c","volume":"258","author":"Pelletier","year":"1992","journal-title":"Science"},{"issue":"16","key":"10.1016\/j.jinorgbio.2025.113182_bb0315","doi-asserted-by":"crossref","first-page":"5940","DOI":"10.1073\/pnas.0306708101","article-title":"Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link","volume":"101","author":"Guo","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"10","key":"10.1016\/j.jinorgbio.2025.113182_bb0320","doi-asserted-by":"crossref","first-page":"3619","DOI":"10.1021\/ja00036a006","article-title":"pH-linked conformational regulation of a metalloprotein oxidation reduction equilibrium - electrochemical analysis of the alkaline form of cytochrome-c","volume":"114","author":"Barker","year":"1992","journal-title":"J. Am. Chem. Soc."},{"issue":"8","key":"10.1016\/j.jinorgbio.2025.113182_bb0325","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1007\/s00775-011-0804-9","article-title":"Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch","volume":"16","author":"Garcia-Heredia","year":"2011","journal-title":"J. Biol. Inorg. Chem."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0330","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1021\/bi00349a024","article-title":"Temperature-dependence of the reduction potential of CuA in carbon-monoxide inhibited cytochrome-c-oxidase","volume":"25","author":"Wang","year":"1986","journal-title":"Biochemistry"},{"issue":"15","key":"10.1016\/j.jinorgbio.2025.113182_bb0335","doi-asserted-by":"crossref","first-page":"E3041","DOI":"10.1073\/pnas.1618008114","article-title":"Structural basis of mitochondrial dysfunction in response to cytochrome c phosphorylation at tyrosine 48","volume":"114","author":"Moreno-Beltr\u00e1n","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0340","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1002\/1439-7633(20020104)3:1<110::AID-CBIC110>3.0.CO;2-2","article-title":"Effect of the protein matrix of cytochrome c in suppressing the inherent peroxidase activity of its heme prosthetic group","volume":"3","author":"Diederix","year":"2002","journal-title":"ChemBioChem"},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.113182_bb0345","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1002\/cbic.200400291","article-title":"The effects of ligand exchange and mobility on the peroxidase activity of a bacterial cytochrome c upon unfolding","volume":"6","author":"Worrall","year":"2005","journal-title":"ChemBioChem"},{"issue":"26","key":"10.1016\/j.jinorgbio.2025.113182_bb0350","doi-asserted-by":"crossref","first-page":"3358","DOI":"10.1021\/acs.biochem.7b00342","article-title":"Effect of a K72A mutation on the structure, stability, dynamics, and peroxidase activity of human cytochrome c","volume":"56","author":"Nold","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0355","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.chemphyslip.2013.11.002","article-title":"Structural transformations of cytochrome c upon interaction with cardiolipin","volume":"179","author":"Muenzner","year":"2014","journal-title":"Chem. Phys. Lipids"},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.113182_bb0360","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1021\/bi00703a036","article-title":"Guanidine-hydrochloride and acid denaturation of horse, cow, and candida-krusei cytochromes-c","volume":"13","author":"Knapp","year":"1974","journal-title":"Biochemistry"},{"issue":"11","key":"10.1016\/j.jinorgbio.2025.113182_bb0365","doi-asserted-by":"crossref","first-page":"4004","DOI":"10.1016\/S0021-9258(17)34790-7","article-title":"Equilibrium and kinetic studies of unfolding of homologous cytochromes c","volume":"253","author":"McLendon","year":"1978","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0370","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1021\/bi981698k","article-title":"Effect of pH on formation of a nativelike intermediate on the unfolding pathway of a Lys 73 --> His variant of yeast iso-1-cytochrome c","volume":"38","author":"Godbole","year":"1999","journal-title":"Biochemistry"},{"issue":"5","key":"10.1016\/j.jinorgbio.2025.113182_bb0375","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1002\/pro.5560070501","article-title":"Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force","volume":"7","author":"McGee","year":"1998","journal-title":"Protein Sci."},{"issue":"12","key":"10.1016\/j.jinorgbio.2025.113182_bb0380","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1016\/j.bbabio.2011.09.012","article-title":"Nitration of tyrosines 46 and 48 induces the specific degradation of cytochrome c upon change of the heme iron state to high-spin","volume":"1807","author":"Diaz-Moreno","year":"2011","journal-title":"BBA-Bioenergetics"},{"issue":"6\u20137","key":"10.1016\/j.jinorgbio.2025.113182_bb0385","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/j.bbabio.2010.03.009","article-title":"Nitration of tyrosine 74 prevents human cytochrome c to play a key role in apoptosis signaling by blocking caspase-9 activation","volume":"1797","author":"Garcia-Heredia","year":"2010","journal-title":"BBA-Bioenergetics"},{"issue":"47","key":"10.1016\/j.jinorgbio.2025.113182_bb0390","doi-asserted-by":"crossref","first-page":"12371","DOI":"10.1021\/bi801329s","article-title":"Effect of nitration on the physicochemical and kinetic features of wild-type and monotyrosine mutants of human respiratory cytochrome c","volume":"47","author":"Rodr\u00edguez-Rold\u00e1n","year":"2008","journal-title":"Biochemistry"},{"issue":"12","key":"10.1016\/j.jinorgbio.2025.113182_bb0395","doi-asserted-by":"crossref","DOI":"10.1002\/pro.5213","article-title":"Phosphorylation of cytochrome c at tyrosine 48 finely regulates its binding to the histone chaperone SET\/TAF-I\u03b2 in the nucleus","volume":"33","author":"Tamargo-Azpilicueta","year":"2024","journal-title":"Protein Sci."},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.113182_bb0400","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.bbabio.2016.01.011","article-title":"Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47","volume":"1857","author":"Guerra-Castellano","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0405","doi-asserted-by":"crossref","first-page":"7100","DOI":"10.1038\/s41467-022-34809-1","article-title":"Phosphorylation disrupts long-distance electron transport in cytochrome c","volume":"13","author":"Gomila","year":"2022","journal-title":"Nat. Commun."},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.113182_bb0410","doi-asserted-by":"crossref","DOI":"10.3390\/cells13060493","article-title":"Phosphorylations and acetylations of cytochrome c control mitochondrial respiration, mitochondrial membrane potential, energy, ros, and apoptosis","volume":"13","author":"Morse","year":"2024","journal-title":"Cells"},{"key":"10.1016\/j.jinorgbio.2025.113182_bb0415","doi-asserted-by":"crossref","DOI":"10.1016\/j.biocel.2020.105704","article-title":"Cytochrome c phosphorylation: control of mitochondrial electron transport chain flux and apoptosis","volume":"121","author":"Kalpage","year":"2020","journal-title":"Int. J. Biochem. Cell Biol."},{"issue":"31","key":"10.1016\/j.jinorgbio.2025.113182_bb0420","doi-asserted-by":"crossref","first-page":"7955","DOI":"10.1073\/pnas.1806833115","article-title":"Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria","volume":"115","author":"Guerra-Castellano","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113182_bb0425","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0006-3495(90)82502-9","article-title":"Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c","volume":"57","author":"Feng","year":"1990","journal-title":"Biophys. J."},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.113182_bb0430","first-page":"1852","article-title":"CIntX: a software tool for calculating the intrinsic exchange rates of labile protons in proteins","volume":"4","author":"Richa","year":"2012","journal-title":"J. Pharm. Sci. Res."},{"issue":"38","key":"10.1016\/j.jinorgbio.2025.113182_bb0435","doi-asserted-by":"crossref","first-page":"8086","DOI":"10.1021\/acs.jpcb.3c04385","article-title":"D2O as an imperfect replacement for H2O: problem or opportunity for protein research?","volume":"127","author":"Giubertoni","year":"2023","journal-title":"J. Phys. Chem. B"},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113182_bb0440","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1002\/bip.20645","article-title":"Stability of globular proteins in H2O and D2O","volume":"85","author":"Efimova","year":"2007","journal-title":"Biopolymers"},{"issue":"16","key":"10.1016\/j.jinorgbio.2025.113182_bb0445","doi-asserted-by":"crossref","first-page":"4461","DOI":"10.1021\/ja00510a003","article-title":"Electrochemistry of horse heart cytochrome-c","volume":"101","author":"Eddowes","year":"1979","journal-title":"J. Am. Chem. Soc."}],"container-title":["Journal of Inorganic Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425003630?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425003630?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,15]],"date-time":"2026-06-15T08:23:51Z","timestamp":1781511831000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0162013425003630"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":89,"alternative-id":["S0162013425003630"],"URL":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.113182","relation":{},"ISSN":["0162-0134"],"issn-type":[{"value":"0162-0134","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes","name":"articletitle","label":"Article Title"},{"value":"Journal of Inorganic Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.113182","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"113182"}}