Abstract
The structural and electronic properties of fluorinated 1-N-arylamino-1-arylmethanephosphonic acid esters were studied and related to the inhibitory effects on NADH:ubiquinone oxidoreductase (complex I). Electrostatic potential surfaces, dipole moments and molecular geometries were analysed. Based on the conformational analysis and the electronic parameters, a simple model for the active site of the fluorinated 1-N-arylamino-1-arylmethanephosphonic acid esters was developed, explaining the inhibitory power. The strongest inhibition effects were found for the 1-(N-4-trifluoromethoxyphenyl)-amino-1-phenylmethanephosphonic acid diethyl ester 1bab.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Binding Sites
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Cattle
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Computer Simulation
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Electrochemistry
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Enzyme Inhibitors / chemistry*
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Enzyme Inhibitors / pharmacology
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Mitochondria, Heart / enzymology
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Mitochondria, Heart / metabolism
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Models, Molecular
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Molecular Conformation
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Molecular Structure*
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NAD(P)H Dehydrogenase (Quinone) / antagonists & inhibitors*
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NAD(P)H Dehydrogenase (Quinone) / chemistry*
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Organophosphorus Compounds / chemistry*
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Organophosphorus Compounds / pharmacology
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Oxygen Consumption
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Protein Conformation
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Software
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Structure-Activity Relationship
Substances
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Enzyme Inhibitors
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Organophosphorus Compounds
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NAD(P)H Dehydrogenase (Quinone)