Investigation of metal-dithiolate fold angle effects: Implications for molybdenum and tungsten enzymes

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 7, 2003, Pages 3719-3724

  Joshi, Hemant K ^a   Cooney, J Jon A ^a   Inscore, Frank E ^a   Gruhn, Nadine E ^a   Lichtenberger, Dennis L ^a   Enemark, John H ^a  

^a University of Arizona   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

METAL; MOLYBDENUM; TUNGSTEN; ALDEHYDE DEHYDROGENASE; ALDEHYDE OXIDASE; DIMETHYL SULFOXIDE REDUCTASE; ENZYME; IRON SULFUR PROTEIN; OXIDOREDUCTASE; THIOL DERIVATIVE; XANTHINE DEHYDROGENASE;

ARTICLE; CATALYSIS; COMPLEX FORMATION; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; MOLECULAR INTERACTION; MOLECULAR MODEL; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; X RAY PHOTOELECTRON SPECTROSCOPY; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM;

ARENE;

ALDEHYDE OXIDASE; ALDEHYDE OXIDOREDUCTASES; BINDING SITES; ENZYMES; IRON-SULFUR PROTEINS; KINETICS; MODELS, MOLECULAR; MOLYBDENUM; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON SULFUR GROUP DONORS; PROTEIN FOLDING; SULFHYDRYL COMPOUNDS; TUNGSTEN; XANTHINE DEHYDROGENASE;

EID: 0037383996     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0636832100     Document Type: Article

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