Open AccessElectron transport in sulfate‐reducing bacteria
Author(s) -
STEWART David E.,
LEGALL Jean,
MOURA Isabel,
MOURA José J. G.,
PECK Harry D.,
XAVIER António V.,
WEINER Paul K.,
WAMPLER John E.
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.tb15168.x
Subject(s) - rubredoxin , desulfovibrio vulgaris , chemistry , cytochrome c , heme , cytochrome , electron transport chain , desulfovibrio , nuclear magnetic resonance spectroscopy , stereochemistry , crystallography , biochemistry , bacteria , sulfate , biology , enzyme , organic chemistry , genetics , mitochondrion
A hypothetical model of the complex formed between the iron‐sulfur protein rubredoxin and the tetraheme cytochrome c 3 from the sulfate‐reducing bacteria Desulfovibrio vulgaris (Hildenborough) has been proposed utilizing computer graphic modeling, computational methods and NMR spectroscopy. The proposed complex appears feasible on the basis of complementary electrostatic interaction and steric factors and is consistent with the data from NMR experiments. In this model, the non‐heme iron atom of rubredoxin is in close proximity to heme 1 of cytochrome c 3 . The complex is stabilized by charge‐pair interactions and hydrogen bonds. This complex is compared to the flavodoxin‐cytochrome c 3 complex previously proposed [Stewart, D. E., LeGall, J., Moura, L., Moura, J. J. G., Peck, H. D. Jr, Xavier, A. V., Weiner, P. K. & Wampler, J. E. (1988) Biochemistry 27 , 2444–2450] and new NMR data shows that both proteins interact with the same heme group of the cytochrome as postulated.