Inhibitor/fatty acid interactions with cytochrome P-450 BM3.
The interaction of fatty acid substrate (palmitate) and inhibitor (metyrapone: 2-methyl-1,2-di-3-pyridyl-1-propanone) with cytochrome P-450 BM3 was analysed by UV-visible and circular dichroism spectroscopy, and by surface-enhanced resonance Raman scattering (SERRS). While visible spectroscopy provides information on the relative affinities of these compounds, SERRS provides additional novel data indicating palmitate-induced structural changes in the haem environment. SERRS also demonstrates that binding of both palmitate and the large nitrogenous ligand metyrapone occurs simultaneously to P-450 BM3 -- highlighting the usefulness of this technique in probing haemoprotein active sites.
Department of Pure and Applied Chemistry, University of Strathclyde, Glasgow, UK.
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Macdonald
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Smith
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Munro
D001426:Bacterial Proteins; D002942:Circular Dichroism; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D008797:Metyrapone / Q000737:chemistry / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase; D019308:Palmitic Acid / Q000737:chemistry / Q000378:metabolism*; D013057:Spectrum Analysis; D013059:Spectrum Analysis, Raman
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D019308:Palmitic Acid; D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases; D008797:Metyrapone