Structural and functional analogue of the active site of polysulfide reductase from Wolinella succinogenes

Inorganic Chemistry

Volumn 43, Issue 15, 2004, Pages 4532-4533

  Nagarajan, Kowliki ^a   Joshi, Hemant K ^b   Chaudhury, Pradeep K ^a   Pal, Kuntal ^a   Cooney, J Jon A ^b   Enemark, John H ^b   Sarkar, Sabyasachi ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

^b University of Arizona   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DITHIOL DERIVATIVE; DITHIOLATE; LIGAND; MOLYBDENUM; OXIDOREDUCTASE; POLYSULFIDE REDUCTASE; SELENIUM; SERINE; SOLVENT; SULFIDE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; COMPLEX FORMATION; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME SYNTHESIS; HYDROPHILICITY; HYDROPHOBICITY; NONHUMAN; REACTION ANALYSIS; STRUCTURE ANALYSIS; WOLINELLA SUCCINOGENES;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; MOLYBDENUM; ORGANOMETALLIC COMPOUNDS; OXIDOREDUCTASES; WOLINELLA;

EID: 3242787234     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic049665i     Document Type: Article

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19. The EPR spectrum as obtained immediately after freezing the reaction mixture changes with time, suggesting the instability of the oxidized product. The native protein displayed varying (g) values depending on the use of varied substrates (see ref 8).