The evolution of the human mitochondrial bc1 complex- adaptation for reduced rate of superoxide production?
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology
Link
https://link.springer.com/content/pdf/10.1007/s10863-023-09957-8.pdf
Reference57 articles.
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2. Bazil JN, Vinnakota KC, Wu F, Beard DA (2013) Analysis of the kinetics and bistability of ubiquinol:cytochrome c oxidoreductase. Biophys J 105:343–355. https://doi.org/10.1016/j.bpj.2013.05.033
3. Berry EA, De Bari H, Huang LS (2013) Unanswered questions about the structure of cytochrome bc1 complexes. Biochim Biophys Acta 1827:1258–1277. https://doi.org/10.1016/j.bbabio.2013.04.006
4. Borek A, Kuleta P, Ekiert R, Pietras R, Sarewicz M, Osyczka A (2015) Mitochondrial disease-related mutation G167P in cytochrome b of Rhodobacter capsulatus Cytochrome bc1 (S151P in Human) affects the equilibrium distribution of [2Fe-2S] cluster and generation of Superoxide. J Biol Chem 290:23781–23792. https://doi.org/10.1074/jbc.M115.661314
5. Borek A, Ekiert R, Osyczka A (2018) Functional flexibility of electron flow between quinol oxidation Qo site of cytochrome bc1 and cytochrome c revealed by combinatory effects of mutations in cytochrome b, iron-sulfur protein and cytochrome c1. Biochim Biophys Acta Bioenerg 1859:754–761. https://doi.org/10.1016/j.bbabio.2018.04.010
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