The membrane-extrinsic domain of cytochrome b558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface

Barbara Schoepp-Cothenet; Michael Schütz; Frauke Baymann; Myriam Brugna; Wolfgang Nitschke; Hannu Myllykallio; Christian Schmidt

doi:10.1016/S0014-5793(00)02357-7

The membrane-extrinsic domain of cytochrome b_558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface

Barbara Schoepp-Cothenet^*, Michael Schütz, Frauke Baymann, Myriam Brugna, Wolfgang Nitschke, Hannu Myllykallio, Christian Schmidt

^*Corresponding author for this work

Institute of Biology

16 Citations (Scopus)

Abstract

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.

Original language	English
Journal	FEBS Letters
Volume	487
Issue number	3
Pages (from-to)	372-376
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/S0014-5793(00)02357-7
Publication status	Published - 05.01.2001

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0014-5793(00)02357-7

Cite this

@article{08df3a1c809b4e16bd9bb317693042d9,

title = "The membrane-extrinsic domain of cytochrome b558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface",

abstract = "The orientation of the membrane-attached cytochrome b558/566-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 b558/566-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 b558/566 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.",

author = "Barbara Schoepp-Cothenet and Michael Sch{\"u}tz and Frauke Baymann and Myriam Brugna and Wolfgang Nitschke and Hannu Myllykallio and Christian Schmidt",

note = "Funding Information: We thank the group of P. Bertrand for extensive access to the EPR facilities, as well as F. Lederer for stimulating discussions in the initial phases of this work. F. Baymann is supported by a FEBS long-term fellowship. M. Sch{\"u}tz benefitted from a post-doctoral position ({\textquoteleft}chercheur associ{\'e}{\textquoteright}) by the CNRS. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.",

year = "2001",

month = jan,

day = "5",

doi = "10.1016/S0014-5793(00)02357-7",

language = "English",

volume = "487",

pages = "372--376",

journal = "FEBS Letters",

issn = "0014-5793",

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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. / Schoepp-Cothenet, Barbara; Schütz, Michael; Baymann, Frauke et al.
In: FEBS Letters, Vol. 487, No. 3, 05.01.2001, p. 372-376.

Research output: Journal Articles › Journal articles › Research › peer-review

TY - JOUR

T1 - The membrane-extrinsic domain of cytochrome b558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface

AU - Schoepp-Cothenet, Barbara

AU - Schütz, Michael

AU - Baymann, Frauke

AU - Brugna, Myriam

AU - Nitschke, Wolfgang

AU - Myllykallio, Hannu

AU - Schmidt, Christian

N1 - Funding Information: We thank the group of P. Bertrand for extensive access to the EPR facilities, as well as F. Lederer for stimulating discussions in the initial phases of this work. F. Baymann is supported by a FEBS long-term fellowship. M. Schütz benefitted from a post-doctoral position (‘chercheur associé’) by the CNRS. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.

PY - 2001/1/5

Y1 - 2001/1/5

N2 - The orientation of the membrane-attached cytochrome b558/566-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 b558/566-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 b558/566 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.

AB - The orientation of the membrane-attached cytochrome b558/566-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 b558/566-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 b558/566 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.

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