Two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H nitroreductase: Description of quantitative structure-activity relationships.

• Authors: Henrikas Nivinskas , Ronald L Koder , Žilvinas Anusevièius , Jonas Šarlauskas , Anne-Frances Miller , Narimantas Čenas
• Languages of publication: EN

Abstracts

EN

Enterobacter cloacae NAD(P)H:nitroreductase catalyzes the reduction of a series of nitroaromatic compounds with steady-state bimolecular rate constants (kcat/Km) ranging from 104 M-1s-1 to 107 M-1s-1 , and oxidizing 2 moles NADH per mole mononitrocompound. Oxidation of excess NADH by polynitrobenzenes including explosives 2,4,6-trinitrotoluene (TNT) and 2,4,6-trinitrophenyl-N-methylnitramine (tetryl), has been observed as a slower secondary process, accompanied by O2 consumption. This type of 'redox cycling' was not related to reactions of nitroaromatic anion-radicals, but was caused by the autoxidation of relatively stable reaction products. The logs kcat/Km of all the compounds examined exhibited parabolic dependence on their enthalpies of single-electron- or two-electron (hydride) reduction, obtained by quantum mechanical calculations. This type of quantitative structure-activity relationships shows that the reactivity of nitroaromatics towards E. cloacae nitroreductase depends mainly on their hydride accepting properties, but not on their particular structure, and does not exclude the possibility of multistep hydride transfer.

Keywords

EN

HMX; nitroreductase; explosive; TNT; electron transfer; tetryl; RDX; pentryl

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2000
• Volume: 47
• Issue: 4
• Pages: 941-949

Dates

published

2000

received

2000-10-3

accepted

2000-11-7

Contributors

author

Henrikas Nivinskas

• Institute of Biochemistry, Mokslininku 12, Vilnius 2600, Lithuania

author

Ronald L Koder

• Department of Chemistry, University of Kentucky, 106 Chemistry-Physics Building, Lexington, KY 40506-0055, U.S.A.

author

Žilvinas Anusevièius

• Institute of Biochemistry, Mokslininku 12, Vilnius 2600, Lithuania

author

Jonas Šarlauskas

• Institute of Biochemistry, Mokslininku 12, Vilnius 2600, Lithuania

author

Anne-Frances Miller

• Department of Chemistry, University of Kentucky, 106 Chemistry-Physics Building, Lexington, KY 40506-0055, U.S.A.

author

Narimantas Čenas

• Institute of Biochemistry, Mokslininku 12, Vilnius 2600, Lithuania

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