Title : Structures of reaction intermediates of bovine cytochrome c oxidase probed by time-resolved vibrational spectroscopy.

Pub. Date : 2000 Nov

PMID : 11132644






5 Functional Relationships(s)
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1 Structures of reaction intermediates of bovine cytochrome c oxidase (CcO) in the reactions of its fully reduced form with O2 and fully oxidized form with H2O2 were investigated with time-resolved resonance Raman (RR) and infrared spectroscopy. Oxygen cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus
2 Structures of reaction intermediates of bovine cytochrome c oxidase (CcO) in the reactions of its fully reduced form with O2 and fully oxidized form with H2O2 were investigated with time-resolved resonance Raman (RR) and infrared spectroscopy. Oxygen cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus
3 Six oxygen-associated RR bands were observed for the reaction of CcO with O2. Oxygen cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus
4 Six oxygen-associated RR bands were observed for the reaction of CcO with O2. Oxygen cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus
5 The reaction of oxidized CcO with H2O2 yields the same oxygen isotope-sensitive bands as those of P and F, indicating the identity of intermediates. Oxygen cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus