Substitutions at position 146 of cytochrome b affect drastically the properties of heme b(L) and the Q(o) site of Rhodobacter capsulatus cytochrome bc1 complex

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1319, Issue 1, 1997, Pages 99-108

  Saribaş, A Sami ^a   Ding, Huangen ^b,c   Dutton, P Leslie ^b   Daldal, Fevzi ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

Cytochrome b; Electron transfer; Mutant; Photosynthesis; Respiration; Ubihydroquinone oxidation site

Indexed keywords

CYTOCHROME B; UBIQUINOL CYTOCHROME C REDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; MUTANT; PHOTOSYNTHESIS; POTENTIOMETRIC TITRATION; PRIORITY JOURNAL; RHODOBACTER CAPSULATUS;

ALANINE; AMINO ACID SEQUENCE; CYTOCHROME B GROUP; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX III; GLYCINE; HEME; KINETICS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RHODOBACTER CAPSULATUS; STRUCTURE-ACTIVITY RELATIONSHIP; UBIQUINONE; VALINE;

EID: 0030936966     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(96)00120-X     Document Type: Article

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