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The membrane‐extrinsic domain of cytochrome b 558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface
Author(s) -
Schoepp-Cothenet Barbara,
Schütz Michael,
Baymann Frauke,
Brugna Myriam,
Nitschke Wolfgang,
Myllykallio Hannu,
Schmidt Christian
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02357-7
Subject(s) - sulfolobus acidocaldarius , cytochrome , chemistry , membrane , electron transfer , redox , crystallography , sulfolobus , biophysics , stereochemistry , biochemistry , photochemistry , archaea , biology , inorganic chemistry , enzyme , gene
The orientation of the membrane‐attached cytochrome b 558/566 ‐haem with respect to the membrane was determined by electron paramagnetic resonance spectroscopy on two‐dimensionally ordered oxidised membrane fragments from Sulfolobus acidocaldarius . Unlike the other redox centres in the membrane, the cytochrome b 558/566 ‐haem was found to cover a range of orientations between 25° and 90°. The described results are reminiscent of those obtained on the Rieske cluster of bc complexes and indicate that the membrane‐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.