1gvr
STUCTURE OF PENTAERYTHRITOL TETRANIRATE REDUCTASE AND COMPLEXED WITH 2,4,6 TRINITROTOLUENE
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OverviewOverview
The reaction of pentaerythritol tetranitrate reductase with reducing and, oxidizing substrates has been studied by stopped-flow spectrophotometry, redox potentiometry, and X-ray crystallography. We show in the reductive, half-reaction of pentaerythritol tetranitrate (PETN) reductase that NADPH, binds to form an enzyme-NADPH charge transfer intermediate prior to, hydride transfer from the nicotinamide coenzyme to FMN. In the oxidative, half-reaction, the two-electron-reduced enzyme reacts with several, substrates including nitroester explosives (glycerol trinitrate and PETN), nitroaromatic explosives (trinitrotoluene (TNT) and picric acid), and, alpha,beta-unsaturated carbonyl compounds (2-cyclohexenone). Oxidation of, the flavin by the nitroaromatic substrate TNT is kinetically, ... [(full description)]
About this StructureAbout this Structure
1GVR is a [Single protein] structure of sequence from [Enterobacter cloacae] with FMN and TNL as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters, and nitroaromatic explosives., Khan H, Harris RJ, Barna T, Craig DH, Bruce NC, Munro AW, Moody PC, Scrutton NS, J Biol Chem. 2002 Jun 14;277(24):21906-12. Epub 2002 Mar 28. PMID:11923299
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