Mechanism of proton transfer inhibition by Cd2+ binding to bacterial reaction centers: Determination of the pKA of functionally important histidine residues

Biochemistry

Volumn 42, Issue 32, 2003, Pages 9626-9632

  Paddock, M L ^a   Sagle, L ^a   Tehrani, A ^b   Beatty, J T ^b   Feher, G ^a   Okamura, M Y ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CADMIUM; CATALYSTS; DISSOCIATION; ELECTROSTATICS; PH EFFECTS; PHOTOSYNTHESIS; REDUCTION;

PROTON TRANSFER;

BIOCHEMISTRY;

ALANINE; CADMIUM; HISTIDINE; IMIDAZOLE DERIVATIVE; QUINOL DERIVATIVE; QUINONE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CYTOPLASM; DISSOCIATION CONSTANT; ELECTRON TRANSPORT; NONHUMAN; PH; PHOTOSYNTHESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTON TRANSPORT; REDUCTION; RHODOBACTER SPHAEROIDES;

ASPARTIC ACID; BINDING SITES; CADMIUM; ELECTRON TRANSPORT; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; PROTEIN BINDING; PROTONS; QUINONES; RECOMBINANT PROTEINS; RHODOBACTER SPHAEROIDES;

BACTERIA (MICROORGANISMS); RHODOBACTER; RHODOBACTER SPHAEROIDES; RHODOPSEUDOMONAS;

EID: 0042527461     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0346648     Document Type: Article

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