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Structure of the respiratory MBS complex reveals iron-sulfur cluster catalyzed sulfane sulfur reduction in ancient life

Author

Listed:
  • Hongjun Yu

    (Van Andel Institute
    Huazhong University of Science and Technology)

  • Dominik K. Haja

    (University of Georgia)

  • Gerrit J. Schut

    (University of Georgia)

  • Chang-Hao Wu

    (University of Georgia)

  • Xing Meng

    (Van Andel Institute)

  • Gongpu Zhao

    (Van Andel Institute)

  • Huilin Li

    (Van Andel Institute)

  • Michael W. W. Adams

    (University of Georgia)

Abstract

Modern day aerobic respiration in mitochondria involving complex I converts redox energy into chemical energy and likely evolved from a simple anaerobic system now represented by hydrogen gas-evolving hydrogenase (MBH) where protons are the terminal electron acceptor. Here we present the cryo-EM structure of an early ancestor in the evolution of complex I, the elemental sulfur (S0)-reducing reductase MBS. Three highly conserved protein loops linking cytoplasmic and membrane domains enable scalable energy conversion in all three complexes. MBS contains two proton pumps compared to one in MBH and likely conserves twice the energy. The structure also reveals evolutionary adaptations of MBH that enabled S0 reduction by MBS catalyzed by a site-differentiated iron-sulfur cluster without participation of protons or amino acid residues. This is the simplest mechanism proposed for reduction of inorganic or organic disulfides. It is of fundamental significance in the iron and sulfur-rich volcanic environments of early earth and possibly the origin of life. MBS provides a new perspective on the evolution of modern-day respiratory complexes and of catalysis by biological iron-sulfur clusters.

Suggested Citation

  • Hongjun Yu & Dominik K. Haja & Gerrit J. Schut & Chang-Hao Wu & Xing Meng & Gongpu Zhao & Huilin Li & Michael W. W. Adams, 2020. "Structure of the respiratory MBS complex reveals iron-sulfur cluster catalyzed sulfane sulfur reduction in ancient life," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19697-7
    DOI: 10.1038/s41467-020-19697-7
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    Cited by:

    1. Hao Leng & Yinzhao Wang & Weishu Zhao & Stefan M. Sievert & Xiang Xiao, 2023. "Identification of a deep-branching thermophilic clade sheds light on early bacterial evolution," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Ralf Steinhilper & Gabriele Höff & Johann Heider & Bonnie J. Murphy, 2022. "Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Yongchan Lee & Outi Haapanen & Anton Altmeyer & Werner Kühlbrandt & Vivek Sharma & Volker Zickermann, 2022. "Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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