含黄素的章鱼碱脱氢酶中铁硫簇的表征

Characterization of iron-sulfur clusters in flavin-containing opine dehydrogenase.

作者信息

Watanabe Seiya, Tajima Kunihiko, Matsui Kazuma, Watanabe Yasuo

机构信息

a Department of Bioscience , Graduate School of Agriculture, Ehime University , Matsuyama , Japan.

b Center for Marine Environmental Studies , Ehime University , Matsuyama , Japan.

出版信息

Biosci Biotechnol Biochem. 2016 Dec;80(12):2371-2375. doi: 10.1080/09168451.2016.1206812. Epub 2016 Jul 7.

DOI:10.1080/09168451.2016.1206812

PMID:27388263

Abstract

Flavin-containing opine dehydrogenase from Bradyrhizobium japonicum forms a heterooligomeric αβγ enzyme complex. An electron paramagnetic resonance spectroscopy analysis using wild-type and site-directed mutants revealed that [4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the γ- and α-subunits, respectively. The latter was found to be important for structural folding and enzyme catalysis.

摘要

来自日本慢生根瘤菌的含黄素的章鱼碱脱氢酶形成一种异源寡聚体αβγ酶复合物。使用野生型和定点突变体进行的电子顺磁共振光谱分析表明，[4Fe-4S]和[2Fe-2S]簇分别结合到γ亚基和α亚基中两种不同类型的[Fe-S]结合位点上。发现后者对结构折叠和酶催化很重要。