title: Barrier compression enhances an enzymatic hydrogen-transfer reaction.
abstract: 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.
authors.affiliation: Manchester Interdisciplinary Biocentre, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester, UK.
authors.forename: Sam
authors.initials: S
authors.lastname: Hay
authors.forename: Christopher R
authors.initials: CR
authors.lastname: Pudney
authors.forename: Tom A
authors.initials: TA
authors.lastname: McGrory
authors.forename: Jiayun
authors.initials: J
authors.lastname: Pang
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Sutcliffe
authors.forename: Nigel S
authors.initials: NS
authors.lastname: Scrutton
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D055162:Biocatalysis; D005486:Flavin Mononucleotide / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry*; D006874:Hydrostatic Pressure; D017136:Ion Transport; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D009243:NAD; D005486:Flavin Mononucleotide; D006859:Hydrogen; D010088:Oxidoreductases; C087820:morphinone reductase