Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase

Biochemistry

Volumn 45, Issue 32, 2006, Pages 9696-9705

  Kappler, Ulrike ^a   Bailey, Susan ^b   Feng, Changjian ^c   Honeychurch, Michael J ^a   Hanson, Graeme R ^a   Bernhardt, Paul V ^a   Tollin, Gordon ^d   Enemark, John H ^c  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b DARESBURY LABORATORY   (United Kingdom)

^c The University of Arizona   (United States)

^d UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; COMPLEXATION; CRYSTALLIZATION; ELECTRON TRANSITIONS; MOLYBDENUM; OXIDATION; SUBSTITUTION REACTIONS; SULFUR;

BACTERIAL SULFITE DEHYDROGENASE; CW-EPR SIGNALS; ELECTRON ACCEPTORS; INTRAMOLECULAR ELECTRON TRANSFER;

PROTEINS;

ARGININE; BACTERIAL ENZYME; HEME; HETERODIMER; LIGAND; MOLYBDENUM; MOLYBDENUM COMPLEX; OXIDOREDUCTASE; OXYGEN; PHENYLALANINE; PROTEIN SUBUNIT; SULFITE; SULFITE DEHYDROGENASE; SULFITE OXIDASE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTINUOUS WAVE ELECTRON PARAMAGNETIC RESONANCE; CRYSTAL STRUCTURE; ELECTRON; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; LASER FLASH PHOTOLYSIS; NONHUMAN; PH; PHOTOLYSIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PURIFICATION; REDUCTION; STARKEYA NOVELLA; THIOBACILLUS;

ALPHAPROTEOBACTERIA; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRONS; HYDROGEN-ION CONCENTRATION; KINETICS; LASERS; MOLYBDENUM; MUTATION; OXIDATION-REDUCTION; OXYGEN; PHOTOLYSIS; SULFITE DEHYDROGENASE; SULFITES; TYROSINE;

BACTERIA (MICROORGANISMS); STARKEYA NOVELLA; VERTEBRATA;

EID: 33747485989     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060058b     Document Type: Article

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