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The structure of the Ni-Fe site in the isolated HoxC subunit of the hydrogen-sensing hydrogenase from Ralstonia eutropha
Citation key ISI:000231350900014
Author Loscher, S and Zebger, I and Andersen, L K and Hildebrandt, P and Meyer-Klaucke, W and Haumann, M
Pages 4287-4291
Year 2005
ISSN 0014-5793
DOI 10.1016/j.febslet.2005.06.063
Address PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
Journal FEBS Lett.
Volume 579
Number 20
Month AUG 15
Publisher ELSEVIER SCIENCE BV
Abstract 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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