Studies on Bioinorganic Chemistry of Cytochrome P-450 Models and Biometal Ions

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  • チトクロムP-450を中心とした金属酵素モデル及び生体関連金属イオンに関する生物無機化学的研究
  • チトクロム P-450 オ チュウシン ト シタ キンゾク コウソ モデル オ

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Abstract

Redox reactions are involved in some fundamental biological processes such as molecular oxygen activation and oxidation of organic compounds by mono-and dioxygenases, electron transfer and enzyme reactions by metalloproteins and biometal ions. To clarify the active site structure and functions of cytochrome P-450, several hydrophilic and lipophilic model compounds were constructed by using metalloporphyrins (Fe-and Coprotoheme or tetraphenylporphyrin) and various types of thiolcontaining ligands. The active site structure of P-450 in the ferric low-spin state was proposed to have a cysteinate thiolate in the 5th position and an oxygen of H2O in the 6th position. Aromatic, aliphatic and olefin oxidation activities were found in the metalloporphyrin-thiol ligand systems under oxygen and the active oxygen species was proposed.<BR>Behaviors of biometal ions such as Mn and V in the living systems were studied on the conversion of the valence states by electron spin resonance spectrometry. Functional and active site models for Mnenzymes such as Mndioxygenase and superoxide dismutase or catalase, respectively, were proposed. In addition, redox and complex reactions of vanadate ion with biomolecules such as cysteine, glutathione, ascorbate, adenosine triphosphate, heme proteins as well as some drugs studied.<BR>This review has been discussed on structure and functions of metalloenzymes and significance of biometal ions.

Journal

  • YAKUGAKU ZASSHI

    YAKUGAKU ZASSHI 106 (8), 619-637, 1986

    The Pharmaceutical Society of Japan

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