SUMMARY: The genes, which encode the four subunits β, γ, δ and α of the [Ni-Fe] hydrogenase from the archaeon , 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 and 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 and gene products are homologous to the - and -encoded subunits of the sulfite reductase enzyme from . This is particularly interesting in view of the recent finding that the hydrogenase appears to be a bifunctional enzyme endowed with both proton- and sulfur- reducing activities.


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