RT Journal Article SR Electronic(1) A1 Pedroni, Paola A1 Volpe, Anna Della A1 Galli, Giuliano A1 Mura, Giovanni M. A1 Pratesi, Claudio A1 Grandi, GuidoYR 1995 T1 Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus : evidence for a relationship to bacterial sulfite reductases JF Microbiology, VO 141 IS 2 SP 449 OP 458 DO https://doi.org/10.1099/13500872-141-2-449 PB Microbiology Society, SN 1465-2080, AB SUMMARY: The hydBGDA genes, which encode the four subunits β, γ, δ and α of the [Ni-Fe] hydrogenase from the archaeon Pyrococcus furiosus , have been isolated and sequenced using a PCR/IPCR-based strategy. From the sequence analysis it appears that the four structural genes are tightly linked and organized in a single transcription unit. The hydD and hydA gene products are related to the small and the large subunits of several archaeal and eubacterial [Ni-Fe] hydrogenases with an overall degree of sequence relatedness ranging from 35% to 50% (identity + similarity). In particular, the amino acid sequence motifs involved in the accommodation of nickel and iron-sulfur clusters are conserved. In addition, the database search revealed that the hydB and hydG gene products are homologous to the asrA - and asrB -encoded subunits of the sulfite reductase enzyme from Salmonella typhimurium . This is particularly interesting in view of the recent finding that the P. furiosus hydrogenase appears to be a bifunctional enzyme endowed with both proton- and sulfur- reducing activities. , UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-141-2-449