Open AccessSpectroscopic characterization of the nickel and iron‐sulphur clusters of hydrogenase from the purple photosynthetic bacterium Thiocapsa roseopersicina
Author(s) -
CAMMACK Richard,
BAGYINKA Csaba,
KOVACS Kornel L.
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb14838.x
Subject(s) - hydrogenase , nickel , electron paramagnetic resonance , redox , chemistry , spectroscopy , metal , crystallography , photochemistry , sulfur , paramagnetism , inorganic chemistry , hydrogen , nuclear magnetic resonance , physics , organic chemistry , quantum mechanics
The thermostable hydrogenase from Thiocapsa roseopersicina was examined by low‐temperature ESR spectroscopy. Two types of signals were detected, from an oxidized iron‐sulphur cluster and a nickel centre (Ni‐A). In the oxidized protein additional signals were observed due to spin‐spin interaction between the two paramagnetic centres. This interaction could be reversibly abolished by reduction to a redox potential below 105 mV. This implies that an additional redox centre is involved in the interaction, for which an Fe 3+ ion is suggested. Reduction with hydrogen induced a second type of nickel ESR signal (Ni‐C), corresponding to an intermediate redox state seen in other nickel hydrogenases. The Ni‐C species was light‐sensitive at cryogenic temperatures. At temperatures near to 4.2 K the Ni‐C signal showed evidence of interaction with another paramagnetic centre, presumably a second iron‐sulphur cluster. On reoxidation a signal due to a third Ni(III) species, Ni‐B, increased in amplitude. These results establish that metal centres in the hydrogenase from T. roseopersicina are closely similar to those of the well‐studied hydrogenase from Chromatium vinosum .