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Volumn 41, Issue 3, 2002, Pages 521-531
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Sterically hindered carboxylate ligands support water-bridged dimetallic centers that model features of metallohydrolase active sites
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINOPEPTIDASE;
CARBOXYLIC ACID;
COBALT;
COBALT COMPLEX;
HYDROLASE;
LIGAND;
METALLOHYDROLASE;
METHIONYL AMINOPEPTIDASE;
NICKEL;
NICKEL COMPLEX;
ORGANOMETALLIC COMPOUND;
UNCLASSIFIED DRUG;
WATER;
ZINC;
ZINC COMPLEX;
ARTICLE;
BINDING SITE;
CHEMICAL STRUCTURE;
CHEMISTRY;
COMPARATIVE STUDY;
COMPLEX FORMATION;
CONFORMATION;
ENZYME ACTIVE SITE;
ENZYMOLOGY;
ESCHERICHIA COLI;
HYDROGEN BOND;
INFRARED SPECTROSCOPY;
METABOLISM;
OXIDATION REDUCTION REACTION;
PHYSICAL CHEMISTRY;
PYROCOCCUS FURIOSUS;
STEREOSPECIFICITY;
STRUCTURE ANALYSIS;
SYNTHESIS;
ULTRAVIOLET SPECTROPHOTOMETRY;
X RAY CRYSTALLOGRAPHY;
AMINOPEPTIDASES;
BINDING SITES;
CARBOXYLIC ACIDS;
CHEMISTRY, PHYSICAL;
COBALT;
CRYSTALLOGRAPHY, X-RAY;
ESCHERICHIA COLI;
HYDROGEN BONDING;
LIGANDS;
MODELS, MOLECULAR;
MOLECULAR CONFORMATION;
MOLECULAR STRUCTURE;
NICKEL;
ORGANOMETALLIC COMPOUNDS;
OXIDATION-REDUCTION;
PYROCOCCUS FURIOSUS;
SPECTROPHOTOMETRY, ULTRAVIOLET;
SPECTROSCOPY, FOURIER TRANSFORM INFRARED;
WATER;
ZINC;
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EID: 0037059870
PISSN: 00201669
EISSN: None
Source Type: Journal
DOI: 10.1021/ic0107431 Document Type: Article |
Times cited : (97)
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References (71)
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