The effect of chloride on the redox and EPR properties of myeloperoxidase.
作者： M Ikeda-Saito , R C Prince
DOI: 10.1016/S0021-9258(17)39470-X
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摘要: Myeloperoxidase was purified from human polymorphonuclear leukocytes and the effect of chloride upon EPR potentiometric properties studied. The redox titration between ferrous ferric states enzyme yielded n = 1 Nernst plots pH 9 4, with clear isosbestic points in optical spectra during change. midpoint potential (Em) forms exhibited a pH-dependent change 4 9, added ion indicated that Cl- competed OH- for binding site on enzyme. Interestingly, dependence Em overall reactions was: myeloperoxidase + 2e- 1H+ myeloperoxidase. rhombic high spin signal which reduced rhombicity chloride. Our results strongly suggest binds to sixth coordination position chlorin iron by replacing water is ligand resting state. It also concluded two centers are identical there no interaction them.
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