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Unusual FTIR and EPR properties of the H 2 ‐activating site of the cytoplasmic NAD‐reducing hydrogenase from Ralstonia eutropha
Author(s) -
Happe Randolph P.,
Roseboom Winfried,
Egert Gabriele,
Friedrich Cornelius G.,
Massanz Christian,
Friedrich Bärbel,
Albracht Simon P.J.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01799-8
Subject(s) - ralstonia , hydrogenase , nad+ kinase , electron paramagnetic resonance , chemistry , cytoplasm , biochemistry , fourier transform infrared spectroscopy , enzyme , nuclear magnetic resonance , physics , quantum mechanics
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.