Yeast cytochrome c peroxidase. Coordination and spin states of heme prosthetic group.
作者： T Yonetani , H Anni
DOI: 10.1016/S0021-9258(18)47968-9
关键词: Chemistry 、 Absorption spectroscopy 、 Spin states 、 Crystallography 、 Ligand field theory 、 Heme 、 Nuclear magnetic resonance 、 Hemeprotein 、 Cytochrome c peroxidase 、 Ligand 、 Electron paramagnetic resonance
摘要: Electronic absorption and electron paramagnetic resonance (EPR) spectroscopic examinations revealed that a freshly prepared cytochrome c peroxidase (CCP) contains penta-coordinated high spin ferric protoheme group. The state of fresh CCP is maintained in remarkably wide range pH (4-8). freezing induces the reversible coordination an internal strong field ligand to heme iron form hexa-coordinated low compound, which shows EPR extrema at gx = 2.70, gy 2.20 gz 1.78. In presence glycerol freezing-induced artifacts are eliminated enzyme exhibits spectrum rhombically distorted axial symmetry with 6.4, 5.3, 1.97 10 K, characteristic enzyme. Upon aging converted due weak iron. This conversion accelerated acidic values, its reversibility varies from fully irreversible depending on degree aging. aging-induced unreactive hydrogen peroxide purely g 6 2 electronic intensified Soret band 408 nm (epsilon 120 mM-1 cm-1) blue-shifted charge-transfer 620 nm. Spectroscopic properties different states aged CCPs compiled order formulate generalized characterization penta- hemoproteins.
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