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The structure of the Ni-Fe site in the isolated HoxC subunit of the hydrogen-sensing hydrogenase from Ralstonia eutropha
Zitatschlüssel Loscher2005
Autor Loscher, S. and Zebger, I. and Andersen, L. K. and Hildebrandt, P. and Meyer-Klaucke, W. and Haumann, M.
Seiten 4287–4291
Jahr 2005
Journal Febs Letters
Jahrgang 579
Nummer 20
Zusammenfassung The regulatory Ni-Fe hydrogenase (RH) from Ralstonia eutropha which forms a [HoxBC](2) complex functions as a hydrogen sensor under aerobic conditions. We have studied a novel Strep-tag isolate of the RH large subunit, HoxC(ST), which lacks the Fe-S clusters of HoxB, allowing for structure determination of the catalytic site by X-ray absorption spectroscopy both at the Ni and, for the first time, also at the Fe K-edge. This technique, together with Fourier-transform infrared spectroscopy, revealed a Ni-Fe site with [O-1(CysS)(2)Ni-II(mu-SCys)(2)Fe-II(CN)(2)(CO)] structure in about 50 % of HoxC(ST) and a [(CysS)(2)Fe-II(CN)(2)(CO)] site lacking Ni in the remainder protein. Possibly both sites may be intermediates in the maturation process of the RH. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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