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Electron transfer by domain movement in cytochrome bc1

Author

Listed:
  • Zhaolei Zhang

    (E. O. Lawrence Berkeley National Laboratory
    The Graduate Group of Biophysics)

  • Lishar Huang

    (E. O. Lawrence Berkeley National Laboratory
    Department of Chemistry University of California)

  • Vladimir M. Shulmeister

    (Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign)

  • Young-In Chi

    (Department of Chemistry University of California)

  • Kyeong Kyu Kim

    (Department of Chemistry University of California)

  • Li-Wei Hung

    (The Graduate Group of Biophysics)

  • Antony R. Crofts

    (This paper is dedicated to the memory of our friend and colleague Vladimir M. Shulmeister, a key member on the project until his untimely death on 27 September 1995)

  • Edward A. Berry

    (Department of Chemistry University of California)

  • Sung-Hou Kim

    (E. O. Lawrence Berkeley National Laboratory
    The Graduate Group of Biophysics
    Department of Chemistry University of California)

Abstract

The cytochrome bc1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe–S protein by ubiquinol. The other site is close enough to cytochrome c1 to allow oxidation of the Fe–S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe–S component in order to shuttle electrons from ubiquinol to cytochrome c1. Such a mechanism has not previously been observed in redox protein complexes.

Suggested Citation

  • Zhaolei Zhang & Lishar Huang & Vladimir M. Shulmeister & Young-In Chi & Kyeong Kyu Kim & Li-Wei Hung & Antony R. Crofts & Edward A. Berry & Sung-Hou Kim, 1998. "Electron transfer by domain movement in cytochrome bc1," Nature, Nature, vol. 392(6677), pages 677-684, April.
    • Handle: RePEc:nat:nature:v:392:y:1998:i:6677:d:10.1038_33612
    DOI: 10.1038/33612
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    1. Daniel Riepl & Ana P. Gamiz-Hernandez & Terezia Kovalova & Sylwia M. Król & Sophie L. Mader & Dan Sjöstrand & Martin Högbom & Peter Brzezinski & Ville R. I. Kaila, 2024. "Long-range charge transfer mechanism of the III2IV2 mycobacterial supercomplex," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Anuj Kumar & Florian Kremp & Jennifer Roth & Sven A. Freibert & Volker Müller & Jan M. Schuller, 2023. "Molecular architecture and electron transfer pathway of the Stn family transhydrogenase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Fangzhu Han & Yiqi Hu & Mengchen Wu & Zhaoxiang He & Hongtao Tian & Long Zhou, 2023. "Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Zhaoxiang He & Mengchen Wu & Hongtao Tian & Liangdong Wang & Yiqi Hu & Fangzhu Han & Jiancang Zhou & Yong Wang & Long Zhou, 2024. "Euglena’s atypical respiratory chain adapts to the discoidal cristae and flexible metabolism," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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