Characterization of steady-state activities of cytochrome c oxidase at alkaline pH: Mimicking the effect of K-channel mutations in the bovine enzyme

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1706, Issue 1-2, 2005, Pages 126-133

  Riegler, David ^a   Shroyer, Lois ^a   Pokalsky, Christine ^a   Zaslavsky, Dmitry ^b   Gennis, Robert ^b   Prochaska, Lawrence J ^a  

^a WRIGHT STATE UNIVERSITY   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Alkaline pH value; Circular dichroism; Cytochrome c; Cytochrome c oxidase; Peroxidase; Steady state kinetics

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME C OXIDASE; HEART ENZYME; HEME; HYDROGEN PEROXIDE; POTASSIUM CHANNEL;

ALKALINITY; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME CONFORMATION; GENE MUTATION; PH; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; REDUCTION; STEADY STATE;

ANIMALS; CATTLE; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX IV; HEME; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; KINETICS; MITOCHONDRIA; MYOCARDIUM; POTASSIUM CHANNELS; SPECTRUM ANALYSIS;

BACTERIA (MICROORGANISMS); BOVINAE;

EID: 11144249354     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.10.002     Document Type: Article

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