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Volumn 40, Issue 15, 2001, Pages 4622-4632
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Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity
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Author keywords
[No Author keywords available]
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Indexed keywords
SUPEROXIDE DISMUTASES;
CATALYSIS;
DIMERS;
ENZYME KINETICS;
HYDROGEN BONDS;
IONIZATION;
MANGANESE;
PH;
PROTEINS;
SPECTROSCOPIC ANALYSIS;
SUBSTRATES;
X RAYS;
BIOCHEMISTRY;
MANGANESE SUPEROXIDE DISMUTASE;
ARTICLE;
CATALYSIS;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME SUBSTRATE COMPLEX;
ESCHERICHIA COLI;
HYDROGEN BOND;
NONHUMAN;
PH;
PRIORITY JOURNAL;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SUBSTITUTION;
BINDING SITES;
CATALYSIS;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ENZYME ACTIVATION;
ESCHERICHIA COLI;
HYDROGEN BONDING;
MANGANESE;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
PHENYLALANINE;
PROTEIN CONFORMATION;
SPECTROPHOTOMETRY, ULTRAVIOLET;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
SUPEROXIDE DISMUTASE;
TYROSINE;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0035901552
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi002403h Document Type: Article |
Times cited : (43)
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References (64)
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