Thermodynamic Redox Properties Governing the Half-Reduction Characteristics of Histamine Dehydrogenase from Nocardioides simplex
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概要
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Histamine dehydrogenase from Nocardioides simplex is a homodimer and belongs to the family of iron-sulfur flavoproteins having one [4Fe-4S] cluster and one 6-S-cysteinyl FMN per monomer. In the reductive titration with histamine, two-electron reduction occurred per monomer at pH<9, while single-electron reduction proceeded at pH>9. The substrate-reduced histamine dehydrogenase yielded an electron paramagnetic resonance spectral signal assigned to the flavin semiquinone. The signal intensity increased with pH up to pH 9 and reached a maximum at pH>9. These unique features are explained in terms of the redox potential of the cofactors, where the redox potential was evaluated over a pH range from 7 to 10 by using a spectroelectrochemical titration method for the flavin and cyclic voltammetry for the [4Fe-4S] cluster. The bell-type pH dependence of the enzymatic activity is also discussed in terms of the pH dependence of the centers’ redox potential.
- 社団法人 日本農芸化学会の論文
著者
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Tsutsumi Maiko
Div. Of Applied Life Sciences Graduate School Of Agriculture Kyoto Univ. Sakyo Kyoto 606-8502 Jpn
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KANO Kenji
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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Shirai Osamu
Division Of Nuclear Engineering Science Research Reactor Institute Kyoto University
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TSUJIMURA Seiya
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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FUJIEDA Nobutaka
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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Tsutsumi Maiko
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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