Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex.

Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex. Research Abstract Details 

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Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex. Abstract Text:

Maiko Tsutsumi,Nobutaka Fujieda,Seiya Tsujimura,Osamu Shirai,Kenji Kano,

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.

Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex. Publishing Authors By Initials

M Tsutsumi,N Fujieda,S Tsujimura,O Shirai,K Kano,

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Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Bioscience, biotechnology, and biochemistry

VOLUME: 72

Page Numbers: 786-96

Journal Abbreviation: Biosci. Biotechnol. Biochem.

ISSN: 1347-6947

DAY: 7

MONTH: 03

YEAR: 2008

Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex. Information

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LANGUAGE: eng

NlmUniqueID: 9205717

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Grant and Affiliation Information for Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex.

AFFILIATION: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.

Country: Japan

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MEDLINETA: Biosci Biotechnol Biochem

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