Unusual FTIR and EPR properties of the H2‐activating site of the cytoplasmic NAD‐reducing hydrogenase from Ralstonia eutropha

FEBS Letters

Egert, Gabriele²  Friedrich, Cornelius G.²  Albracht, Simon P.J.¹  Friedrich, Bärbel³  Happe, Randolph P.¹  Massanz, Christian³  Roseboom, Winfried¹ 

[1] E.C. Slater Institute, Biochemistry, University of Amsterdam, Plantage Muidergracht 12, NL-1018 TV Amsterdam, The Netherlands;Lehrstuhl Technische Mikrobiologie, Universität Dortmund, Emil-Figge-Strasse 66, D-44221 Dortmund, Germany;Institut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany

关键词: [NiFe]-hydrogenase;    Active site;    Cyanide;    Carbon monoxide;    Ralstonia eutropha;    SH;    soluble (cytoplasmic) hydrogenase;    BV;    benzyl viologen;    MV;    methyl viologen;    EPR;    electron paramagnetic resonance;    FTIR;    Fourier-transform infrared spectroscopy;    XAS;    X-ray absorption spectroscopy;    EXAFS;    extended X-ray absorption fine structure;   

DOI  :  10.1016/S0014-5793(99)01799-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Soluble NAD-reducing [NiFe]-hydrogenase (SH) from Ralstonia eutropha (formerly Alcaligenes eutrophus) has an infrared spectrum with one strong band at 1956 cm⁻¹ and four weak bands at 2098, 2088, 2081 and 2071 cm⁻¹ in the 2150–1850 cm⁻¹ spectral region. Other [NiFe]-hydrogenases only show one strong and two weak bands in this region, attributable to the NiFe(CN)₂(CO) active site. The position of these three bands is highly sensitive to redox changes of the active site. In contrast, reduction of the SH resulted in a shift to lower frequencies of the 2098 cm⁻¹ band only. These and other properties prompted us to propose the presence of a Ni(CN)Fe(CN)₃(CO) active site.

【 授权许可】

Unknown