Mechanism of hydrogen peroxide dismutation by a dimanganese catalase mimic: Dominant role of an intramolecular base on substrate binding affinity and rate acceleration

Inorganic Chemistry

Volumn 39, Issue 14, 2000, Pages 3020-3028

  Boelrijk, A E M ^a   Dismukes, G C ^a  

^a PRINCETON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID; CATALASE; GLUTAMIC ACID; HYDROGEN PEROXIDE; HYDROXIDE; HYDROXYL RADICAL; MANGANESE; MANGANESE DERIVATIVE; OXYGEN;

ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL BOND; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; KINETICS; MICHAELIS CONSTANT; MOLECULAR MIMICRY; OXIDATION; OXIDATION REDUCTION POTENTIAL; PROTON TRANSPORT; REACTION ANALYSIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

CATALASE; CATALYSIS; HYDROGEN PEROXIDE; KINETICS; MANGANESE; MOLECULAR MIMICRY; SUBSTRATE SPECIFICITY; THERMUS THERMOPHILUS;

EID: 0034631699     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic9911771     Document Type: Article

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