Biochemical analysis of the soluble hydrogenase from the thermophilic organism revealed that the enzyme is an aß tetramer, with the a and ß subunits having a molecular mass of 50 kDa and 25 kDa, respectively. The most important biochemical properties of the enzyme are a specific activity of 77 μmol min (mg protein) a for methylviologen of 0.2 mM, a pH optimum of 7.5 and a of about 70 †C. In addition, the enzyme is remarkably stable to oxygen inactivation, retaining full activity after 24 h exposure to air. By using oligodeoxynucleotides designed on the basis of the N-terminal sequences of the two subunits, the corresponding genes have been isolated and sequenced. When compared to the other hydrogenases so far characterized, the hydrogenase appears to be a typical [Ni-Fe] enzyme. The hydrogenase was expressed in at high levels in a soluble form but it was not active. The analysis of the recombinant large subunit showed that it was not post-translationally processed at its C-terminus.


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