The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase

European Journal of Biochemistry

Volumn 261, Issue 2, 1999, Pages 379-391

  Döpner, Susanne ^a   Hildebrandt, Peter ^a,d   Rosell, Federico I ^b   Mauk, A Grant ^b   Von Walter, Matthias ^c   Buse, Gerhard ^c   Soulimane, Tewfik ^c  

^a MAX PLANCK INSTITUTE   (Germany)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^c RWTH AACHEN UNIVERSITY   (Germany)

^d MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

Author keywords

Cytochrome c; Cytochrome c oxidase; Electron transfer; Resonance Raman

Indexed keywords

ALANINE; CYTOCHROME C; CYTOCHROME C OXIDASE; ISOENZYME; LYSINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; ELECTROCHEMISTRY; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STABILITY; MOLECULAR MODEL; PRIORITY JOURNAL; RAMAN SPECTROMETRY; STEADY STATE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ALANINE; ANIMALS; BINDING SITES; CATTLE; CYTOCHROME C GROUP; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX IV; HEME; KINETICS; LYSINE; MODELS, MOLECULAR; MUTATION; PHOSPHOLIPIDS; POLYLYSINE; PROTEIN CONFORMATION; SPECTRUM ANALYSIS, RAMAN;

BOVINAE;

EID: 0033561331     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00249.x     Document Type: Article

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