HupUV proteins of Rhodobacter capsulatus can bind H2: evidence from the H-D exchange reaction
HupUV proteins of Rhodobacter capsulatus can bind H2: evidence from the H-D exchange reaction
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荚膜红杆菌的 HupUV 蛋白可以结合 H2：来自 H-D 交换反应的证据
DOI：
10.1128/jb.179.1.290-292.1997
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发表时间：
1997
影响因子：
3.2
通讯作者：
S. Elsen
中科院分区：
文献类型：
--
作者：
P. Vignais;B. Dimon;N. Zorin;A. Colbeau;S. Elsen
用D2-H2O体系测定了缺乏hupSL编码的氢化酶的荚膜红杆菌JP 91和R. capsulatus BSE 16，其缺乏HupUV蛋白。从质粒pAC 206表达的hupUV基因产物显示催化H-D交换反应，该H-D交换反应与由于膜结合的hupSL编码的氢化酶引起的H-D交换反应不同。在O2存在下，BSE 16细胞的摄取氢化酶催化系统中存在的H2、D2和HD的快速摄取和氧化，并且其活性（H-D交换，还原甲基紫精[MV+]存在下的H2释放）依赖于外部pH，而HupUV引起的H-D交换对外部pH和O2保持不敏感。这些数据表明，HupSL二聚体是周质取向的，而HupUV蛋白在细胞质区室中。
The H-D exchange reaction has been measured with the D2-H2O system, for Rhodobacter capsulatus JP91, which lacks the hupSL-encoded hydrogenase, and R. capsulatus BSE16, which lacks the HupUV proteins. The hupUV gene products, expressed from plasmid pAC206, are shown to catalyze an H-D exchange reaction distinguishable from the H-D exchange due to the membrane-bound, hupSL-encoded hydrogenase. In the presence of O2, the uptake hydrogenase of BSE16 cells catalyzed a rapid uptake and oxidation of H2, D2, and HD present in the system, and its activity (H-D exchange, H2 evolution in presence of reduced methyl viologen [MV+]) depended on the external pH, while the H-D exchange due to HupUV remained insensitive to external pH and O2. These data suggest that the HupSL dimer is periplasmically oriented, while the HupUV proteins are in the cytoplasmic compartment.
使用 Desulfovibrio baculatus 的 77Se 富集 (NiFeSe) 氢化酶进行 EPR 研究。
DOI：
--
发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
He,SH;Teixeira,M;LeGall,J;Patil,DS;Moura,I;Moura,JJ;DerVartanian,DV;Huynh,BH;PeckJr,HD
通讯作者：
PeckJr,HD