Structural Evidence that Peroxiredoxin Catalytic Power is Based on Transition-State Stabilization

Journal of Molecular Biology

Volumn 402, Issue 1, 2010, Pages 194-209

  Hall, Andrea ^a   Parsonage, Derek ^b   Poole, Leslie B ^b   Karplus, P Andrew ^a  

^a OREGON STATE UNIVERSITY   (United States)

^b WAKE FOREST SCHOOL OF MEDICINE   (United States)

Author keywords

Catalytic power; Dithiothreitol; Peroxiredoxin; Transition state stabilization

Indexed keywords

CYSTEINE; DITHIOTHREITOL; OXYGEN; PEROXIDE; PEROXIREDOXIN; WATER;

ARTICLE; CATALYSIS; COMPETITIVE INHIBITION; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME STRUCTURE; HYDROGEN BOND; MICROENVIRONMENT; NONHUMAN; PEROXIDATION; PRIORITY JOURNAL; STEREOCHEMISTRY; SUBSTITUTION REACTION; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DITHIOTHREITOL; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXYGEN; PEROXIDES; PEROXIREDOXINS; PROTEIN CONFORMATION;

EID: 77956171017     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.022     Document Type: Article

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