Premium
Barrier Compression Enhances an Enzymatic Hydrogen‐Transfer Reaction
Author(s) -
Hay Sam,
Pudney Christopher R.,
McGrory Tom A.,
Pang Jiayun,
Sutcliffe Michael J.,
Scrutton Nigel S.
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200805502
Subject(s) - flavin mononucleotide , chemistry , hydrostatic pressure , catalysis , flavin group , active site , enzyme catalysis , hydrogen bond , chemical physics , photochemistry , thermodynamics , molecule , enzyme , organic chemistry , physics
Putting the squeeze on : Hydrostatic pressure causes a shortening of the charge‐transfer bond in the binary complex of morphinone reductase and NADH 4 (see diagram). Molecular dynamics simulations suggest that pressure reduces the average reaction barrier width by restricting the conformational space available to the flavin mononucleotide and NADH within the active site. The apparent rate of catalysis increases with pressure.