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In a recent review article Babcok and Wikstrom (Nature, 1992, 356, 301–309) proposed that the species of cytochrome- c -oxidase which binds molecular oxygen during turnover is the so-called mixed valence enzyme, in which the binuclear center cytoch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ef249da3190f30afe856a8054a54a75
https://hdl.handle.net/11590/132454
https://hdl.handle.net/11590/132454
Cytochrome oxidase (EC 1.9.3.1; ferrocytochrome c:oxygen oxidoreductase) was studied during steady-state by optical and e.p.r. methods. Starting with either the ‘resting’ or the ‘pulsed’ enzyme, oxidase, cytochrome c, ascorbate and O2 were mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38e8ead1cef73b8b3aab9dc4551275f1
https://europepmc.org/articles/PMC1158254/
https://europepmc.org/articles/PMC1158254/
Publikováno v:
The Biochemical journal. 215(2)
The reaction of Neurospora crassa cytochrome c oxidase with CO was studied by flash-photolysis and rapid-mixing experiments, leading to the determination of the association and dissociation rate constants (7 X 10(4) M-1 X s-1 and 0.02s-1 respectively