Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/2226
DC FieldValueLanguage
dc.contributor.authorBabcock, Gerald T.-
dc.contributor.authorVarotsis, Constantinos-
dc.date.accessioned2013-01-23T13:11:31Zen
dc.date.accessioned2013-05-16T06:25:30Z-
dc.date.accessioned2015-12-02T09:16:09Z-
dc.date.available2013-01-23T13:11:31Zen
dc.date.available2013-05-16T06:25:30Z-
dc.date.available2015-12-02T09:16:09Z-
dc.date.issued1993-04-
dc.identifier.citationJournal of bioenergetics and biomembranes, 1993, vol. 25, no. 2, pp. 71-80en_US
dc.identifier.issn15736881-
dc.identifier.urihttps://hdl.handle.net/20.500.14279/2226-
dc.description.abstractThe kinetic constraints that are imposed on cytochrome oxidase in its dual function as the terminal oxidant in the respiratory process and as a redox- linked proton pump provide a unique opportunity to investigate the molecular details of biological O2 activation. By using flow/flash techniques, it is possible to visualize individual steps in the O2-binding and reduction process, and results from a number of spectroscopic investigations on the oxidation of reduced cytochrome oxidase by O2 are now available. In this article, we use these results to synthesize a reaction mechanism for O2 activation in the enzyme and to simulate time-concentration profiles for a number of intermediates that have been observed experimentally. Kinetic manifestation of the consequences of coupling exergonic electron transfer to endergonic proton translocation emerge from this analysis. Energetic efficiency in this process apparently requires that potentially toxic intermediate oxidation states of dioxygen accumulate to substantial concentration during the reduction reactionen_US
dc.language.isoenen_US
dc.relation.ispartofJournal of Βioenergetics and Βiomembranesen_US
dc.rights© Springeren_US
dc.subjectCytochrome oxidaseen_US
dc.subjectHemoproteinsen_US
dc.subjectOxygenen_US
dc.subjectElectron transporten_US
dc.subjectOxidation-reduction reactionen_US
dc.titleDiscrete steps in dioxygen activation - the cytochrome oxidase/O2 reactionen_US
dc.typeArticleen_US
dc.affiliationMichigan State Universityen
dc.collaborationMichigan State Universityen_US
dc.journalsHybrid Open Accessen_US
dc.countryUnited Statesen_US
dc.subject.fieldSocial Sciencesen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1007/BF00762849en_US
dc.dept.handle123456789/54en
dc.relation.issue2en_US
dc.relation.volume25en_US
cut.common.academicyear2020-2021en_US
dc.identifier.spage71en_US
dc.identifier.epage80en_US
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.cerifentitytypePublications-
item.openairetypearticle-
crisitem.journal.journalissn1573-6881-
crisitem.journal.publisherSpringer Nature-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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