CONSERVATION OF HYDROGENASE AND POLYFERREDOXIN STRUCTURES IN THE HYPERTHERMOPHILIC ARCHAEBACTERIUM METHANOTHERMUS-FERVIDUS

被引：29

作者：

STEIGERWALD, VJ ^{[1
]}

BECKLER, GS ^{[1
]}

REEVE, JN ^{[1
]}

机构：

[1] OHIO STATE UNIV,DEPT MICROBIOL,COLUMBUS,OH 43210

来源：

JOURNAL OF BACTERIOLOGY | 1990年 / 172卷 / 08期

关键词：

D O I：

10.1128/jb.172.8.4715-4718.1990

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A 3.3-kilobase-pair region of the Methanothermus fervidus genome encoding part of the small subunit and all of the large subunit of the methyl viologen-reducing hydrogenase and a polyferredoxin was cloned and sequenced. The sequence of this hyperthermophilic hydrogenase conforms to the consensus sequence established for procaryotic [NiFe] hydrogenases. Although the M. fervidus polyferredoxin is the same size as the Methanobacterium thermoautotrophicum ferredoxin, containing six tandemly arranged bacterial ferredoxinlike domains, these two proteins are predicted to be only 64% identical in their primary sequences.

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页码：4715 / 4718

页数：4

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