Solvent-Slaved protein motions accompany proton but not hydride tunneling in light-activated protochlorophyllide oxidoreductase

Angewandte Chemie - International Edition

Volumn 48, Issue 21, 2009, Pages 3850-3853

  Heyes, Derren J ^a   Sakuma, Michiyo ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Enzymes; Hydride transfer; Proton transfer; Reaction mechanisms; Solvent dynamics

Indexed keywords

DYNAMIC NETWORK; ENZYME ACTIVE SITES; HYDRIDE TRANSFER; HYDRIDE TRANSFERS; PROTEIN MOTION; PROTOCHLOROPHYLLIDE; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; REACTION MECHANISMS; REDUCTION REACTION; SOLVENT DYNAMICS;

CATALYSTS; CHLOROPHYLL; ENZYMES; SOLVENTS;

PROTON TRANSFER;

HYDROGEN; OXIDOREDUCTASE; PROTOCHLOROPHYLLIDE REDUCTASE; PROTON; SOLVENT;

CHEMICAL STRUCTURE; CHEMISTRY; CYANOBACTERIUM; ENZYME ACTIVATION; ENZYMOLOGY; LIGHT; METABOLISM; PHOTOCHEMISTRY; RADIATION RESPONSE; VISCOSITY;

CYANOBACTERIA; ENZYME ACTIVATION; HYDROGEN; LIGHT; MOLECULAR STRUCTURE; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PHOTOCHEMICAL PROCESSES; PROTONS; SOLVENTS; VISCOSITY;

EID: 70349976864     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200900086     Document Type: Article

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