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dc.creatorPopović, Dragan
dc.date.accessioned2019-01-30T17:34:33Z
dc.date.available2019-01-30T17:34:33Z
dc.date.issued2013
dc.identifier.issn0939-4451
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/1195
dc.description.abstractThe function of cytochrome c oxidase as a biomolecular nanomachine that transforms energy of redox reaction into protonmotive force across a biological membrane has been subject of intense research, debate, and controversy. The structure of the enzyme has been solved for several organisms; however details of its molecular mechanism of proton pumping still remain elusive. Particularly, the identity of the proton pumping site, the key element of the mechanism, is still open to dispute. The pumping mechanism has been for a long time one of the key unsolved issues of bioenergetics and biochemistry, but with the accelerating progress in this field many important details and principles have emerged. Current advances in cytochrome oxidase research are reviewed here, along with a brief discussion of the most complete proton pumping mechanism proposed to date, and a molecular basis for control of its efficiency.en
dc.publisherSpringer Wien, Wien
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172035/RS//
dc.rightsrestrictedAccess
dc.sourceAmino Acids
dc.subjectCytochrome c oxidaseen
dc.subjectProton pumping mechanismen
dc.subjectKinetic controlen
dc.subjectProton-coupled electron transferen
dc.subjectCatalytic cycleen
dc.subjectBioenergeticsen
dc.subjectRedox-driven proton pumpen
dc.titleCurrent advances in research of cytochrome c oxidaseen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractПоповић, Драган;
dc.citation.volume45
dc.citation.issue5
dc.citation.spage1073
dc.citation.epage1087
dc.citation.other45(5): 1073-1087
dc.citation.rankM22
dc.identifier.pmid23999646
dc.identifier.doi10.1007/s00726-013-1585-y
dc.identifier.rcubConv_3046
dc.identifier.scopus2-s2.0-84886288179
dc.identifier.wos000325813800005
dc.type.versionpublishedVersion


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