The intrinsic stability of the second intermediate following the dioxygen-bound form in the O2 reduction by cytochrome c oxidase

FEBS Letters

Volumn 570, Issue 1-3, 2004, Pages 161-165

  Oda, Kenji ^a,b   Ogura, Takashi ^a,b   Appelman, Evan H ^c   Yoshikawa, Shinya ^b  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF HYOGO   (Japan)

^c ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

CcO, cytochrome c oxidase; Cytochrome c oxidase; FO, fully oxidized; FR, fully reduced; MV, mixed valence; Oxygen activation; P intermediate; Proton pump; Resonance Raman; RR, resonance Raman; TR 3, time resolved resonance Raman

Indexed keywords

CYTOCHROME C OXIDASE; OXYGEN;

AERATION; ALKALINITY; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME METABOLISM; ENZYME STABILITY; NONHUMAN; OXIDATION KINETICS; OXYGEN AFFINITY; PH MEASUREMENT; PRIORITY JOURNAL; PROTON TRANSPORT; RAMAN SPECTROMETRY; REDUCTION;

ANIMALS; CATTLE; ELECTRON TRANSPORT COMPLEX IV; ELECTRONS; HYDROGEN-ION CONCENTRATION; MYOCARDIUM; OXYGEN; PROTEIN BINDING; PROTONS; SPECTRUM ANALYSIS, RAMAN; TIME FACTORS;

EID: 3142570449     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.06.036     Document Type: Article

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