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J Bacteriol, July 1998, p. 3719-3723, Vol. 180, No. 14
Laboratoire de Bioénergétique et
Ingénierie des Protéines (UPR 9036),
Received 16 March 1998/Accepted 17 May 1998
The Rieske 2Fe2S cluster of Chlorobium limicola forma
thiosulfatophilum strain tassajara was studied by electron
paramagnetic resonance spectroscopy. Two distinct orientations of its g
tensor were observed in oriented samples corresponding to differing
conformations of the protein. Only one of the two conformations
persisted after treatment with
2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone. A redox
midpoint potential (Em) of +160 mV in the pH
range of 6 to 7.7 and a decreasing Em (
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Diversity of Cytochrome bc Complexes:
Example of the Rieske Protein in Green Sulfur Bacteria
60 to
80 mV/pH unit) above pH 7.7 were found. The implications of the
existence of differing conformational states of the Rieske protein, as
well as of the shape of its Em-versus-pH curve,
in green sulfur bacteria are discussed.
*
Corresponding author. Mailing address: Laboratoire de
Bioénergétique et Ingénierie des Protéines (UPR
9036), Institut de Biologie Structurale et Microbiologie, 31 chemin
Joseph Aiguier, 13402 Marseille Cedex 20, France. Phone: (33) 4 91164435. Fax: (33) 4 91164578. E-mail:
nitschke{at}ibsm.cnrs-mrs.fr.
J Bacteriol, July 1998, p. 3719-3723, Vol. 180, No. 14
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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