Characterization of the gene encoding the [Fe]-hydrogenase from Megasphaera elsdenii

被引:33
作者
Atta, M [1 ]
Meyer, J [1 ]
机构
[1] CEA Grenoble, Dept Biol Mol & Struct, F-38054 Grenoble, France
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1476卷 / 02期
关键词
iron-sulfur; metalloenzyme; electron transfer; evolution; ferredoxin;
D O I
10.1016/S0167-4838(99)00245-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The gene encoding the [Fe]-hydrogenase from the anaerobic bacterium Megasphaera elsdenii has been cloned and sequenced. The gene is monocistronic, in keeping with the protein being a monomer. The translated protein sequence (484 residues, M-r = 53 kDa) comprises a small 2[4Fe-4S] ferredoxin-like domain and a large domain containing the catalytic site. Comparisons with other [Fe]-hydrogenase sequences, including two of which the crystal structures are known, show that the M. elsdenii protein is among the smallest of these enzymes and provide useful indications regarding the basic structural core common to all [Fe]-hydrogenases. It is, nevertheless, to be noted that the genome of Thermotoga maritima encodes a putative [Fe]-hydrogenase that would consist of only 301 residues. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:368 / 371
页数:4
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