{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T01:46:16Z","timestamp":1790473576995,"version":"4.1.0"},"reference-count":33,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2020,10,8]],"date-time":"2020-10-08T00:00:00Z","timestamp":1602115200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012190","name":"Ministry of Science and Higher Education of the Russian Federation","doi-asserted-by":"publisher","award":["\u2116 \u0410\u0410\u0410\u0410-\u041019-119071190045-0"],"award-info":[{"award-number":["\u2116 \u0410\u0410\u0410\u0410-\u041019-119071190045-0"]}],"id":[{"id":"10.13039\/501100012190","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomimetics"],"abstract":"<jats:p>The oxidation of ascorbic acid by air oxygen and hydrogen peroxide in the presence of the copper-binding compound (cbc) from bacteria Methylococcus capsulatus (M) was studied. The rate constant of ascorbic acid oxidation by air oxygen in the presence of the copper complex with cbc from M. capsulatus (M) was shown to be 1.5 times higher than that of the noncatalytic reaction. The rate constant of ascorbic acid oxidation by hydrogen peroxide in the presence of the copper complex with cbc from M. capsulatus (M) decreased by almost one-third compared to the reaction in the absence of the copper complex with cbc. It was assumed that cbc can be involved in a multilevel system of antioxidant protection and can protect a bacterial cell from oxidation stress. Thus, the cbc is mimetic ascorbate oxidase in the oxidation of ascorbic acid by molecular oxygen.<\/jats:p>","DOI":"10.3390\/biomimetics5040048","type":"journal-article","created":{"date-parts":[[2020,10,8]],"date-time":"2020-10-08T08:52:41Z","timestamp":1602147161000},"page":"48","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Oxidation of L-Ascorbic Acid in the Presence of the Copper-Binding Compound from Methanotrophic Bacteria Methylococcus capsulatus (M)"],"prefix":"10.3390","volume":"5","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8844-417X","authenticated-orcid":false,"given":"Lidia V.","family":"Avdeeva","sequence":"first","affiliation":[{"name":"Institute of Problems of Chemical Physics of RAS, Academician Semenov Ave. 1, Chernogolovka 142432, Moscow Region, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rudolf I.","family":"Gvozdev","sequence":"additional","affiliation":[{"name":"Institute of Problems of Chemical Physics of RAS, Academician Semenov Ave. 1, Chernogolovka 142432, Moscow Region, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,10,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1128\/MMBR.00058-15","article-title":"Methanobactin and the link between copper and bacterial methane oxidation","volume":"80","author":"DiSpirito","year":"2016","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.molcatb.2008.09.005","article-title":"Hydrogen peroxide as an effecter on the inactivation of particulate methane monooxygenase under aerobic conditions","volume":"57","author":"Miyaji","year":"2009","journal-title":"J. Mol. Catal. B-Enzym."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1134\/S0026261709060022","article-title":"Antioxidant systems of moderately thermophilic methanotrophs Methylocaldum szegediense and Methylococcus capsulatus","volume":"78","author":"Medvedkova","year":"2009","journal-title":"Microbiology"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.febslet.2004.06.064","article-title":"Oxygen-dependent H2O2 production by Rubisco","volume":"571","author":"Kim","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1134\/S0026261708010165","article-title":"Synthesis of melanin by a moderately thermophilic methanotroph Methylocaldum szegediense depends on cultivation temperature","volume":"77","author":"Medvedkova","year":"2008","journal-title":"Microbiology"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1016\/j.jinorgbio.2008.02.003","article-title":"Oxidase, superoxide dismutase, and hydrogen peroxide reductase activities of methanobactin from types I and II methanotrophs","volume":"102","author":"Choi","year":"2008","journal-title":"J. Inorg. Biochem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"e02289-17","DOI":"10.1128\/AEM.02289-17","article-title":"Metals and methanotrophy","volume":"84","author":"Semrau","year":"2018","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1134\/S0003683815020088","article-title":"Biosynthesis of secondary metabolites in methanotrophs: Biochemical and genetic aspects (Review)","volume":"51","author":"Khmelenina","year":"2015","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1016\/j.jinorgbio.2010.08.002","article-title":"Spectral and thermodynamic properties of methanobactin from \u03b3-proteobacterial methane oxidizing bacteria: A case for copper competition on a molecular level","volume":"104","author":"Choi","year":"2010","journal-title":"J. Inorg. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"e1700041","DOI":"10.1126\/sciadv.1700041","article-title":"Methylmercury uptake and degradation by methanotrophs","volume":"3","author":"Lu","year":"2017","journal-title":"Sci. Adv."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1128\/jb.178.4.1018-1029.1996","article-title":"Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)","volume":"178","author":"Zahn","year":"1996","journal-title":"J. Bacteriol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3417","DOI":"10.1099\/mic.0.28169-0","article-title":"Effect of methanobactin on the activity and electron paramagnetic resonance spectra of the membrane-associated methane monooxygenase in Methylococcus capsulatus Bath","volume":"151","author":"Choi","year":"2005","journal-title":"Microbiology"},{"key":"ref_13","first-page":"132","article-title":"Optimization cultivation of bacteria Methylococcus capsulatus (M) for production methanobactin","volume":"11","author":"Avdeeva","year":"2015","journal-title":"Nat. Tech. Sci."},{"key":"ref_14","first-page":"101","article-title":"Isolation and purification of methanobactin from Methylococcus capsulatus (M)","volume":"280","author":"Avdeeva","year":"2013","journal-title":"FEBS J."},{"key":"ref_15","first-page":"95","article-title":"Spectral-fluorescent properties of methanobactin from Methylococcus capsulatus (strain M)","volume":"2","author":"Avdeeva","year":"2016","journal-title":"Acta Nat."},{"key":"ref_16","unstructured":"Pozin, M.E. (1951). Hydrogen Peroxide and Peroxide Compounds, Goskhimizdat. (In Russian)."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1134\/S0036024412070266","article-title":"The kinetics of oxidation of bilirubin and ascorbic acid in solution","volume":"86","author":"Solomonov","year":"2012","journal-title":"Russ. J. Phys. Chem. A"},{"key":"ref_18","unstructured":"Dawson, R., Elliot, D., Elliot, W., and Jones, K. (1986). Data for Biochemical Research, Clarendon."},{"key":"ref_19","first-page":"43","article-title":"Oxidation of ascorbic acid by molecular oxygen in the presence of heterobimetallic complexes of copper","volume":"75","author":"Yatsimirsky","year":"2009","journal-title":"Ukr. Chem. J."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1271\/bbb.61.1693","article-title":"Formation mechanism of monodehydro-l-ascorbic acid and superoxide anion in the autoxidation of l-ascorbic acid","volume":"61","author":"Miyake","year":"1997","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"4176","DOI":"10.1021\/ja00992a036","article-title":"Metal ion and metal chelate catalyzed oxidation of ascorbic acid by molecular oxygen. I. Cupric and ferric ion catalyzed oxidation","volume":"89","author":"Khan","year":"1967","journal-title":"J. Am. Chem. Soc."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1590\/S0103-50532006000200021","article-title":"Kinetic studies of the oxidation of L-ascorbic acid by tris(oxalate)cobaltate in the presence of CDTA metal ion complexes","volume":"17","author":"Moya","year":"2006","journal-title":"J. Braz. Chem. Soc."},{"key":"ref_23","first-page":"433","article-title":"The influence of transition metal ions on the kinetics of ascorbic acid oxidation by methylene blue in strongly acidic media","volume":"25","author":"Khan","year":"2001","journal-title":"Turk. J. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1016\/j.crci.2011.08.008","article-title":"Kinetics and mechanism of oxidation of L-ascorbic acid by peroxomonosulphate in acid perchlorate medium. Role of copper (II) as a trace metal-ion catalyst","volume":"14","author":"Sailani","year":"2011","journal-title":"CR Chim."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1265","DOI":"10.1039\/dt9900001265","article-title":"Role of trace metal ions. Kinetics and mechanism of the copper(II)-catalysed oxidation of ascorbic acid with peroxodiphosphate in acetate buffers","volume":"4","author":"Mishra","year":"1990","journal-title":"J. Chem. Soc. Dalton Trans."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.2116\/analsci.16.1317","article-title":"Chemiluminescence studies of the oxidation of ascorbic acid with copper(II) catalyzed by halide anions and its application to the determination of halide anions and ascorbic acid","volume":"16","author":"Zhang","year":"2000","journal-title":"Anal. Sci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1097\/01.CCM.0000186787.64500.12","article-title":"Reactive oxygen species","volume":"33","year":"2005","journal-title":"Crit. Care Med."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/S0277-5387(00)83175-7","article-title":"Reactions of L-ascorbic acid with transition metal complexes","volume":"11","author":"Davies","year":"1992","journal-title":"Polyhedron"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1134\/S0965544112050076","article-title":"Iron and copper complexes with nitrogen-containing ligands as catalysts for cyclohexane oxidation with hydrogen peroxide under mild reaction conditions","volume":"52","author":"Maksimov","year":"2012","journal-title":"Petrol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1134\/S0965544108030080","article-title":"Benzene oxidation with hydrogen peroxide catalyzed by soluble and heterogenized copper compounds","volume":"48","author":"Takaki","year":"2008","journal-title":"Petrol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"110","DOI":"10.19261\/cjm.2017.404","article-title":"Effect of copper concentration on the growth of Methylococcus capsulatus (strain M)","volume":"12","author":"Avdeeva","year":"2017","journal-title":"Chem. J. Mold."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1371\/journal.pbio.0020303","article-title":"Genomic insights into methanotrophy: The complete genome sequence of Methylococcus capsulatus (Bath)","volume":"2","author":"Ward","year":"2004","journal-title":"PLoS Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1007\/s002030050510","article-title":"Cytochrome c peroxidase from Methylococcus capsulatus Bath","volume":"168","author":"Zahn","year":"1997","journal-title":"Arch. Microbiol."}],"container-title":["Biomimetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2313-7673\/5\/4\/48\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:17:18Z","timestamp":1760177838000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2313-7673\/5\/4\/48"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,10,8]]},"references-count":33,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2020,12]]}},"alternative-id":["biomimetics5040048"],"URL":"https:\/\/doi.org\/10.3390\/biomimetics5040048","relation":{},"ISSN":["2313-7673"],"issn-type":[{"value":"2313-7673","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,10,8]]}}}