Parallel pathways and free-energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure

ChemBioChem

Volumn 10, Issue 8, 2009, Pages 1379-1384

  Pudney, Christopher R ^a   McGrory, Tom ^b   Lafite, Pierre ^a   Pang, Jiayun ^b   Hay, Sam ^a   Leys, David ^a   Sutcliffe, Michael J ^b   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Catalysis; Enzymes; Flavoproteins; Hydride transfer; Hydrostatic pressure

Indexed keywords

CARBOXYL GROUP; ENZYME; HYDRIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; FLAVINE MONONUCLEOTIDE; HYDROGEN; MORPHINONE REDUCTASE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; CATALYSIS; CHEMICAL REACTION; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME KINETICS; HYDROSTATIC PRESSURE; MOLECULAR DYNAMICS; MUTANT; PRIORITY JOURNAL; SIMULATION; SPECTROSCOPY; WILD TYPE; AMINO ACID SUBSTITUTION; BIOCATALYSIS; CHEMISTRY; COMPUTER SIMULATION; KINETICS; METABOLISM; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS; TRANSPORT AT THE CELLULAR LEVEL; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BIOCATALYSIS; BIOLOGICAL TRANSPORT; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; FLAVIN MONONUCLEOTIDE; HYDROGEN; HYDROSTATIC PRESSURE; KINETICS; MUTANT PROTEINS; NAD; OXIDOREDUCTASES; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 67651148171     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200900071     Document Type: Article

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