The membrane-extrinsic domain of cytochrome b(558/566) from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface
B. Schoepp-cothenet et al., The membrane-extrinsic domain of cytochrome b(558/566) from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface, FEBS LETTER, 487(3), 2001, pp. 372-376
The orientation of the membrane-attached cytochrome b(558/566)-haem with re
spect to the membrane was determined by electron paramagnetic resonance spe
ctroscopy on two-dimensionally ordered oxidised membrane fragments from Sul
folobus acidocaldarius. Unlike the other redox centres in the membrane, the
cytochrome b(558/566)-haem mas found to cover a range of orientations betw
een 25 degrees and 90 degrees. The described results are reminiscent of tho
se obtained on the Rieske cluster of bc complexes and indicate that the mem
brane-extrinsic domain of cytochrome b(558/566) can perform pivoting motion
between two extreme positions. Such a conformational flexibility is likely
to play a role in electron transfer with its redox partners. (C) 2001 Fede
ration of European Biochemical Societies. Published by Elsevier Science B.V
. All rights reserved.