Conservation of hydrogenase and polyferredoxin structures in the hyperthermophilic archaebacterium Methanothermus fervidus.
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.
Steigerwald
V J
VJ
Department of Microbiology, Ohio State University, Columbus 43210.
Beckler
G S
GS
Reeve
J N
JN
D000595:Amino Acid Sequence; D001105:Archaea / Q000235:genetics*; D001419:Bacteria / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D019605:Euryarchaeota / Q000235:genetics*; D005288:Ferredoxins / Q000235:genetics*; D005798:Genes, Bacterial; D006358:Hot Temperature; D006864:Hydrogenase / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family; D011485:Protein Binding
D005288:Ferredoxins; D006864:Hydrogenase