Characterization of a HoxEFUYH type of NiFe hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module

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	Characterization of a HoxEFUYH type of NiFe hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module
	Long, M. N. ; Liu, J. J. ; Chen, Z. F. ; Bleijlevens, B. ; Roseboom, W. ; Albracht, S. P. J. ; Long MN(龙敏南)
刊名	http://dx.doi.org/10.1007/s00775-006-0162-1
	2007-01
关键词	RESPIRATORY COMPLEX-I ELECTRON-PARAMAGNETIC-RESONANCE NADH-UBIQUINONE OXIDOREDUCTASE MEMBRANE-BOUND HYDROGENASE CLUSTER-FREE HYDROGENASE RAY-STRUCTURE ANALYSIS NOCARDIA-OPACA 1B FE ACTIVE-SITE 2 FMN GROUPS CHROMATIUM-VINOSUM
英文摘要	A soluble hydrogenase from Allochromatium vinosum was purified. It consisted of a large (M-r = 52 kDa) and a small (M-r = 23 kDa) subunit. The genes encoding for both subunits were identified. They belong to an open reading frame where they are preceded by three more genes. A DNA fragment containing all five genes was cloned and sequenced. The deduced amino acid sequences of the products characterized the complex as a member of the HoxEFUYH type of [NiFe] hydrogenases. Detailed sequence analyses revealed binding sites for eight Fe-S clusters, three [2Fe-2S] clusters and five [4Fe-4S] clusters, six of which are also present in homologous subunits of [FeFe] hydrogenases and NADH:ubiquione oxidoreductases (complex I). This makes the HoxEFUYH type of hydrogenases the one that is evolutionary closest to complex I. The relative positions of six of the potential Fe-S clusters are predicted on the basis of the X-ray structures of the Clostridium pasteurianum [FeFe] hydrogenase I and the hydrophilic domain of complex I from Thermus thermophilus. Although the HoxF subunit contains binding sites for flavin mononucleotide and NAD(H), cell-free extracts of A. vinosum did not catalyse a H-2-dependent reduction of NAD(+). Only the hydrogenase module (HoxYH) could be purified. Its electron paramagnetic resonance (EPR) and IR spectral properties showed the presence of a Ni-Fe active site and a [4Fe-4S] cluster. Its activity was sensitive to carbon monoxide. No EPR signals from a light-sensitive Ni-a-C* state could be observed. This study presents the first IR spectroscopic data on the HoxYH module of a HoxEFUYH type of [NiFe] hydrogenase.
语种	英语
内容类型	期刊论文
源URL	[http://dspace.xmu.edu.cn/handle/2288/65975]
专题	生命科学－已发表论文
推荐引用方式 GB/T 7714	Long, M. N.,Liu, J. J.,Chen, Z. F.,et al. Characterization of a HoxEFUYH type of NiFe hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module[J]. http://dx.doi.org/10.1007/s00775-006-0162-1,2007.
APA	Long, M. N..,Liu, J. J..,Chen, Z. F..,Bleijlevens, B..,Roseboom, W..,...&龙敏南.(2007).Characterization of a HoxEFUYH type of NiFe hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module.http://dx.doi.org/10.1007/s00775-006-0162-1.
MLA	Long, M. N.,et al."Characterization of a HoxEFUYH type of NiFe hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module".http://dx.doi.org/10.1007/s00775-006-0162-1 (2007).