Open AccessCharacterization of the cytochrome system of a nitrogen‐fixing strain of a sulfate‐reducing bacterium: Desulfovibrio desulfuricans strain Berre‐Eau
Author(s) -
MOURA Isabel,
FAUQUE Guy,
LeGALL Jean,
XAVIER Antonio V.,
MOURA José
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb10674.x
Subject(s) - desulfovibrio , cytochrome , electron paramagnetic resonance , cytochrome c , chemistry , strain (injury) , dithionite , sulfate reducing bacteria , heme , sodium dithionite , bacteria , nuclear chemistry , biochemistry , sulfate , nuclear magnetic resonance , inorganic chemistry , biology , organic chemistry , enzyme , physics , genetics , mitochondrion , anatomy
Two c ‐type cytochromes were purified and characterized by electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopic techniques, from the sulfate‐reducer nitrogen‐fixing organism, Desulfovibrio desulfuricans strain Berre‐Eau (NCIB 8387). The purification procedures included several chromatographic steps on alumina, carboxymethylcellulose and gel filtration. A tetrahaem and a monohaem cytochrome were identified. The multihaem cytochrome has visible, EPR and NMR spectra with general properties similar to other low‐potential bis‐histidinyl axially bound haem proteins, belonging to the class of tetrahaem cytochrome c 3 isolated from other Desulfovibrio species. The monohaem cytochrome c 553 is ascorbate‐reducible and its EPR and NMR data are characteristic of a cytochrome with methionine‐histidine ligation. Their properties are compared with other homologous proteins isolated from sulfate‐reducing bacteria.