Conservation of primary structure in prokaryotic hydrogenases |
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Authors: | John N Reeve Gregory S Beckler |
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Institution: | Department of Microbiology, The Ohio State University, Columbus, OH, U.S.A. |
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Abstract: | Abstract All prokaryotic (NiFe)-hydrogenases so far studied at the primary sequence level appear to have evolved from a common ancestral sequence. Highly conserved cysteinyl and histidinyl residues indicate regions likely to be essential for enzyme activity, ligand and co-factor binding. There is a very highly conserved sequence over 100 basepairs (bp) in length within the intergenic region upstream of the methyl-viologen hydrogenase encoding genes in several different strains of Methanobacterium thermoautotrophicum , indicating that a sequence of this length is needed to direct and regulate the expression of these genes. |
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Keywords: | Nickel binding Methanobacterium thermoautotrophicum Archaebacteria Methanogen Gene evolution Methyl viologen-reducing hydrogenase |
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