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Structural insight into the type-II mitochondrial NADH dehydrogenases

Author

Listed:
  • Yue Feng

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Wenfei Li

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Jian Li

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Jiawei Wang

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Jingpeng Ge

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Duo Xu

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Yanjing Liu

    (State Key Laboratory of Systematic and Evolutionary Botany, Institute of Botany, Chinese Academy of Sciences)

  • Kaiqi Wu

    (Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China)

  • Qingyin Zeng

    (State Key Laboratory of Systematic and Evolutionary Botany, Institute of Botany, Chinese Academy of Sciences)

  • Jia-Wei Wu

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Changlin Tian

    (Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China
    High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, China)

  • Bing Zhou

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Maojun Yang

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University)

Abstract

Analysis of the respective crystal structures of the yeast single-component type-II NADH dehydrogenase Ndi1 in its substrate-free form and when bound to NADH, ubiquinone and NADH–ubiquinone shows that Ndi1 homodimerization through its carboxy-terminal domain is critical for its catalytic activity and membrane targeting.

Suggested Citation

  • Yue Feng & Wenfei Li & Jian Li & Jiawei Wang & Jingpeng Ge & Duo Xu & Yanjing Liu & Kaiqi Wu & Qingyin Zeng & Jia-Wei Wu & Changlin Tian & Bing Zhou & Maojun Yang, 2012. "Structural insight into the type-II mitochondrial NADH dehydrogenases," Nature, Nature, vol. 491(7424), pages 478-482, November.
    • Handle: RePEc:nat:nature:v:491:y:2012:i:7424:d:10.1038_nature11541
    DOI: 10.1038/nature11541
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    Cited by:

    1. Yun Lv & Chunhui Liang & Qichao Sun & Jing Zhu & Haiyan Xu & Xiaoqing Li & Yao-yao Li & Qihai Wang & Huiqing Yuan & Bo Chu & Deyu Zhu, 2023. "Structural insights into FSP1 catalysis and ferroptosis inhibition," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Meng-Shu Hao & Anna M Jensen & Ann-Sofie Boquist & Yun-Jun Liu & Allan G Rasmusson, 2015. "The Ca2+-Regulation of the Mitochondrial External NADPH Dehydrogenase in Plants Is Controlled by Cytosolic pH," PLOS ONE, Public Library of Science, vol. 10(9), pages 1-17, September.
    3. Blanca Jiménez-Gómez & Patricia Ortega-Sáenz & Lin Gao & Patricia González-Rodríguez & Paula García-Flores & Navdeep Chandel & José López-Barneo, 2023. "Transgenic NADH dehydrogenase restores oxygen regulation of breathing in mitochondrial complex I-deficient mice," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    4. Da-Yun Jin & Xuejie Chen & Yizhou Liu & Craig M. Williams & Lars C. Pedersen & Darrel W. Stafford & Jian-Ke Tie, 2023. "A genome-wide CRISPR-Cas9 knockout screen identifies FSP1 as the warfarin-resistant vitamin K reductase," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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