pH and microwave power effects on the electron spin resonance spectra of Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase.

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概要

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• The present study shows that the electron spin resonance (ESR.) spectral features of Rhus laccase depend considerably on the pH value of the enzyme solution and the irradiated microwave power. Because of the local protein structure change, the type 1 copper is appreciably autoreduced at alkaline pH as monitored both by the ESR and absorption spectroscopies. In addition, the ESR signal of the type 2 copper, especially its g⊥ region, becomes prominent at alkaline pH. Protein dissociation from a water or an imidazole group coordinated to the type 2 copper is supposed to be responsible for this behavior. Besides above pH effects, the g⊥ component of the type 2 copper ESR signal is obscured with rising microwave power level. The power saturation behavior of native laccase and its derivatives reveals that the type 2 copper is more easily saturated than the type 1 copper. Cucumis ascorbate oxidase also exhibits similar behavior upon pH variation and microwave power saturation.

• 社団法人 日本生化学会の論文

著者

• Chikira Makoto

  Department Of Applied Chemistry Chuo University

• Sakurai Takeshi

  ollege of Liberal Arts and Sciences, Kanazawa University

• Suzuki Shinnichiro

  College of General Education, Osaka University

関連論文

• Synthesis of New Cationic Schiff Base Complexes of Copper(II) and Their Selective Binding with DNA
• pH and microwave power effects on the electron spin resonance spectra of Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase.

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