Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase.
Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase.
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日本慢生根瘤菌膜结合氢化酶的氢泛醌氧化还原酶活性。
DOI：
10.1111/j.1574-6968.1993.tb06331.x
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发表时间：
1993
影响因子：
2.1
通讯作者：
Maier,RJ
中科院分区：
文献类型：
--
作者：
Ferber,DM;Maier,RJ
缓生根瘤菌japan - rhizobium umheterodi二聚体镍铁氢化酶高效催化h2 -泛素-1氧化还原酶活性，其速率可达人工电子受体亚甲基蓝最大速率的47%。凝胶过滤层析和sds -聚丙烯酰胺凝胶电泳实验表明，纯化后的酶为异源二聚体，仅含有65 kDa和33 kDa亚基。还原-氧化吸收差谱显示不存在可检测的细胞色素。纯化的异二聚体氢化酶和膜的h2 -泛素-1氧化还原酶活性被2-n-庚基-4-羟基喹啉-n-氧化物和抗霉素A显著抑制，这两种抑制剂已知作用于电子传递链的醌区。我们的研究结果是第一个用纯化的氢化酶测定h2 -泛醌氧化还原酶活性的报道。
TheBradyrhizobium japonicumheterodimeric nickel-iron hydrogenase efficiently catalyzed H2-ubiquinone-1 oxidoreductase activity at rates up to 47% of the maximal rates obtained using the artificial electron acceptor methylene blue. Gel filtration chromatography and SDS-polyacrylamide gel electrophoresis experiments demonstrated that the purified enzyme was a heterodimer containing only the 65 kDa and 33 kDa subunits. Reduced minus oxidized absorption difference spectra demonstrated the absence of detectable cytochromes. The H2-ubiquinone-1 oxidoreductase activity of both the purified heterodimeric hydrogenase and membranes was significantly inhibited by 2-n-heptyl-4-hydroxyquinoline-N-oxide and antimycin A, inhibitors known to act in the quinone region of electron transport chains. Our results are the first report of H2-ubiquinone oxidoreductase activity by a purified hydrogenase.