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Catalysis of NO production by a molybdoenzyme model
J Murray1, D Macartney, G R Thatcher
1Department of Chemistry, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Abstract:
[reaction--see text] Nitric oxide (NO) is an important biological messenger molecule. Nitrates, including nitroglycerin (GTN), are clinically important vasodilators believed to be biotransformed in vivo to NO, a 3e(-) reduction. Molybdenum hydrotris-(3,5-dimethyl-1-pyrazolyl) borate complex (MoTPB) was shown to be an efficient catalyst of GTN degradation, with triphenylphosphine (Ph(3)P) acting as reducing cofactor, producing significant amounts of NO. MoTPB/Ph(3)P is an excellent enzyme model system, showing the feasibility of nitrate biotransformation mediated by a molybdoenzyme.
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