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Conservation of hydrogenase and polyferredoxin structures in the hyperthermophilic archaebacterium Methanothermus
V J Steigerwald1, G S Beckler, J N Reeve
1Department of Microbiology, Ohio State University, Columbus 43210.
Journal of Bacteriology
|August 1, 1990
Abstract:
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.