SEISAN KENKYU
Online ISSN : 1881-2058
Print ISSN : 0037-105X
ISSN-L : 0037-105X
Research Review
Study of the Electronic States of the [Ni-Fe] and [Ni-Fe-Se] Hydrogenase Active Center
Takafumi KURODAToshiyuki HIRANOFumitoshi SATO
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2012 Volume 64 Issue 3 Pages 345-350

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Abstract
A hydrogenase(Hase) is an enzyme that catalyzes the reversible redox reaction between hydrogen ion and hydrogen. Hase is easily inactivated under an oxygen atmosphere. The[Ni-Fe-Se]-Hase is more stabilized against oxygen molecules than the[Ni-Fe]-Hase. The former, however, has a selenocysteine nearby the active site; therefore the large-scale production is difficult by protein engineering. The calculations of the electron structures of[Ni-Fe]- and[Ni-Fe-Se]-Hases have been carried out, in order to clarify mechanism of the inactivation reaction. Consequently, not only selenocystein but also the nearest-neighbor amino acid residues on the active site have contributed to the stabilization. In other words, the[Ni-Fe]-Hase, which has no selenocystein, has possibilities to stabilize against oxygen molecule by amino acids substitution. This study will provide a new design for industrial application of Hase.
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© 2012 Institute of Industrial Science The University of Tokyo
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