TY - JOUR A1 - D'Imprima, Edoardo A1 - Mills, Deryck J. A1 - Parey, Kristian Kurt A1 - Brandt, Ulrich A1 - Kühlbrandt, Werner A1 - Zickermann, Volker A1 - Vonck, Janet T1 - Cryo-EM structure of respiratory complex I reveals a link to mitochondrial sulfur metabolism T2 - Biochimica et Biophysica Acta N2 - Mitochondrial complex I is a 1MDa membrane protein complex with a central role in aerobic energy metabolism. The bioenergetic core functions are executed by 14 central subunits that are conserved from bacteria to man. Despite recent progress in structure determination, our understanding of the function of the ~30 accessory subunits associated with the mitochondrial complex is still limited. We have investigated the structure of complex I from the aerobic yeast Yarrowia lipolytica by cryo-electron microscopy. Our density map at 7.9Å resolution closely matches the 3.6-3.9Å X-ray structure of the Yarrowia lipolytica complex. However, the cryo-EM map indicated an additional subunit on the side of the matrix arm above the membrane surface, pointing away from the membrane arm. The density, which is not present in any previously described complex I structure and occurs in about 20 % of the particles, was identified as the accessory sulfur transferase subunit ST1. The Yarrowia lipolytica complex I preparation is active in generating H2S from the cysteine derivative 3-mercaptopyruvate, catalyzed by ST1. We thus provide evidence for a link between respiratory complex I and mitochondrial sulfur metabolism. KW - Complex I KW - Cryo-electron microscopy KW - Electron transport chain KW - Mitochondria KW - NADH:ubiquinone oxidoreductase KW - Sulfur metabolism Y1 - 2016 UR - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/41813 UR - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-418133 SN - 0005-2728 N1 - © 2016 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). VL - 1857 IS - 12 SP - 1935 EP - 1942 ER -