Complex I (NADH:ubiquinone oxidoreductase) is the first and largest protein complex of the oxidative phosphorylation. Crystal structures have elucidated the positions of most subunits of bacterial evolutionary origin in the complex, but the positions of the eukaryotic subunits are unknown. Based on the analysis of sequence conservation we propose intra-molecular disulfide bridges and the inter-membrane space localization of three Cx9C-containing subunits in human: NDUFS5, NDUFB7 and NDUFA8. We experimentally confirm the localization of the latter two, while our data are consistent with disulfide bridges in NDUFA8. We propose these subunits stabilize the membrane domain of complex I. Structured summary: NDUFA8 and NDUFS3 physically interact by blue native page (View interaction) © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Szklarczyk, R., Wanschers, B. F. J., Nabuurs, S. B., Nouws, J., Nijtmans, L. G., & Huynen, M. A. (2011). NDUFB7 and NDUFA8 are located at the intermembrane surface of complex i. FEBS Letters, 585(5), 737–743. https://doi.org/10.1016/j.febslet.2011.01.046