Blocking the K-pathway still allows rapid one-electron reduction of the binuclear center during the anaerobic reduction of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1797, Issue 6-7, 2010, Pages 619-624

  Ganesan, Krithika ^a   Gennis, Robert B ^a  

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

Author keywords

Cytochrome oxidase; K pathway; Protons; R. sphaeroides; Respiration

Indexed keywords

CUPROUS ION; CYTOCHROME C OXIDASE; HEME; POTASSIUM CHANNEL; PROTON; THREONINE;

ANAEROBIC METABOLISM; ARTICLE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GENE MUTATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; RHODOBACTER SPHAEROIDES; SITE DIRECTED MUTAGENESIS; STEADY STATE; STOICHIOMETRY;

AMINO ACID SUBSTITUTION; ANAEROBIOSIS; BACTERIAL PROTEINS; BASE SEQUENCE; DNA PRIMERS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX IV; HEME; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; OXIDATION-REDUCTION; PROTONS; RECOMBINANT PROTEINS; RHODOBACTER SPHAEROIDES;

RHODOBACTER SPHAEROIDES;

EID: 77953812499     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.03.012     Document Type: Article

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