Wolinella succinogenes quinol:fumarate reductase - 2.2-Å resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer

Biochimica et Biophysica Acta - Biomembranes

Volumn 1565, Issue 2, 2002, Pages 215-231

  Lancaster, C RoyD ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

Atomic model; Bioenergetics; Fumarate reductase; Membrane protein; Transmembrane electrochemical potential; X ray crystallography

Indexed keywords

ALCOHOL DERIVATIVE; CYTOCHROME B; FLAVOPROTEIN; FUMARATE REDUCTASE; HEME; HYDROGENASE; HYDROXYL GROUP; IRON SULFUR PROTEIN; MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEIN SUBUNIT; QUINOL:FUMARATE REDUCTASE; SERINE; UNCLASSIFIED DRUG;

CATALYSIS; CRYSTAL STRUCTURE; ELECTROCHEMISTRY; ELECTRON; ELECTRON TRANSPORT; HYDROPHILICITY; HYPOTHESIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTON TRANSPORT; REVIEW; SITE DIRECTED MUTAGENESIS; WOLINELLA SUCCINOGENES; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME B GROUP; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX IV; INTRACELLULAR MEMBRANES; MEMBRANE PROTEINS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR STRUCTURE; OXIDOREDUCTASES; PROTEIN CONFORMATION; VITAMIN K 2; WOLINELLA;

WOLINELLA; WOLINELLA SUCCINOGENES;

EID: 0037064218     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(02)00571-0     Document Type: Review

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