CJCU

Chem. J. Chinese Universities ›› 2001, Vol. 22 ›› Issue (7): 1137.

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EPR Study of Soluble Hydrogenase from Photosynthetic Bacteria Chromatium vinosum

LONG Min-Nan1, SU Wen-Jin1, Albracht-S. P. J.2, ZHANG Feng-Zhang1, XU Liang-Shu1   

  1. 1. The Key Laboratory of Bioorganic Phosphorus Chemistry, Ministry of Education, Department of Chemistry, School of Life Sciences and Engineering, Tsinghua University, Beijing 100084, China;
    2. E.C.SlaterInstitute University of Amsterdam, Amsterdam, the Netherlands
  • Received:2000-06-14 Online:2001-07-24 Published:2001-07-24

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Abstract: Asoluble hydrogenase(SH) was purified from Chromatium vinosum by five step chromatography(DE-23, TSK-DEAE(I), Ultragel AcA-44, TSK-DEAE(Ⅱ), Superdex TM75) with a specific activity of 8.4 μmol H2/(min·mg prot). The oxidized SHyield two Ni(Ⅲ) EPR(electron paramagnetic resonance) signals( gx,y,z = 2.37, 2.16, 2.016 and gx,y,z = 2.30, 2.23, 2.016 ) at 45 Kwhich occurred in the other NiFe-hydrogenases. However, no[3Fe-4S] cluster EPRsignal was obtained at 10 K. When the SHwas reduced by H2 (over night at 8 ℃), the Ni(Ⅲ) EPRsignals disappeared, and an EPR signal from a reduced[4Fe-4S] cluster appeared( gx,y,z = 1.88, 1.90, 2.045). The results show that the soluble hydrogenase from C.vinosum is a new NiFe hydrogenase which catalyzes H2 production.

Key words: Chromatium vinosum, Soluble hydrogenase, EPR spectra

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