Effects of Mutation of the Conserved Lysine-362 in Cytochrome c Oxidase from Rhodobacter sphaeroides

We describe the effects of a mutation, K362M, of the conserved lysine in cytochrome c oxidase from Rhodobacter sphaeroides, a residue located in a putative proton channel that may convey substrate protons to the binuclear center. Spectra of the “as prepared”, ferricyanide-oxidized, and dithionite-re...

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Veröffentlicht in:	Biochemistry (Easton) 1997-11, Vol.36 (47), p.14456-14464
Hauptverfasser:	Jünemann, Susanne, Meunier, Brigitte, Gennis, Robert B, Rich, Peter R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Binding Sites Conserved Sequence Electron Spin Resonance Spectroscopy Electron Transport Complex IV - chemistry Electron Transport Complex IV - metabolism Lysine Mutagenesis, Site-Directed Oxidation-Reduction Protein Conformation Rhodobacter sphaeroides - enzymology Spectrophotometry
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