![]() furiosus and show that the α subunit contains the NiFe-catalytic site. The deduced sequences of the two subunits (Mbh 11 and 12) were distinctly different from those of the four subunits that comprise each of the two cytoplasmic NiFe-hydrogenases of P. ![]() Using N-terminal amino acid sequence information, the genes proposed to encode the α and β subunits were located in the genome database within a putative 14-gene operon (termed mbh). furiosus ferredoxin as an electron carrier, nor did either catalyze the reduction of elemental sulfur with H 2 as the electron donor. Neither highly washed membranes nor the purified enzyme used NAD(P)(H) or P. The reduced enzyme gave rise to an electron paramagnetic resonance signal typical of the so-called Ni-C center of mesophilic NiFe-hydrogenases. The purified preparation contained two major proteins (α and β) in an approximate 1:1 ratio with a minimum molecular mass near 65 kDa and contained ∼1 Ni and 4 Fe atoms/mol. The enzyme was solubilized with n-dodecyl-β- d-maltoside and purified by multistep chromatography in the presence of Triton X-100. Highly washed membrane preparations from cells of the hyperthermophilic archaeon Pyrococcus furiosus contain high hydrogenase activity (9.4 μmol of H 2 evolved/mg at 80☌) using reduced methyl viologen as the electron donor.
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