Conserved nonliganding residues of the Rhodobacter capsulatus rieske iron-sulfur protein of the bc1 complex are essential for protein structure, properties of the [2Fe-2S] cluster, and communication with the quinone pool

Biochemistry

Volumn 36, Issue 39, 1997, Pages 11675-11684

  Liebl, Ursula ^a,b   Sled, Vladimir ^c   Brasseur, Gaël ^a,d   Ohnishi, Tomoko ^c   Daldal, Fevzi ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b LABORATOIRE D OPTIQUE APPLIQUÉE   (France)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d AIX MARSEILLE UNIVERSITY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; IRON SULFUR PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PHOTOSYNTHESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; RHODOBACTER CAPSULATUS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BENZOQUINONES; CATTLE; CONSERVED SEQUENCE; ELECTRON TRANSPORT COMPLEX III; ESCHERICHIA COLI; IRON-SULFUR PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RHODOBACTER CAPSULATUS; SEQUENCE ALIGNMENT;

ATTA; BACTERIA (MICROORGANISMS); BOVINAE; RHODOBACTER CAPSULATUS; RHODOPSEUDOMONAS;

EID: 0030874771     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi970776l     Document Type: Article

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