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Wiseman, B., Nitharwal, R.G., Fedotovskaya, O., Schäfer, J., Guo, H., Kuang, Q., Benlekbir, S., Sjöstrand, D., Ädelroth, P., Rubinstein, J.L., Brzezinski, P. and Högbom, M. (Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden)
The respiratory chain powers the synthesis of ATP in aerobic organisms. In mycobacteria, electrons are transferred from respiratory complex III to menaquinol, which passes them on to complex IV where the terminal acceptor, oxygen, is reduced. Respiratory complexes III and IV couple electron transfer to proton translocation across the membrane, establishing an electrochemical proton gradient that drives e.g. ATP synthesis. In recent years, the respiratory chain of Mycobacteria has been identified as a potential target for new antibiotics. Here, we isolated and characterized a functional respiratory supercomplex from M. smegmatis. We found that the supercomplex from M. smegmatis contains an active superoxide dismutase (SOD). An accessory subunit with an apparent ATPase motif was identified as a part of the supercomplex. Direct electron transfer from respiratory complex III to IV of M. smegmatis is facilitated by an intrinsic di-heme cytochrome cc subunit. This subunit was resolved in the structure in both its closed and open conformation, indicating a role as an electrical switch between the respiratory complexes. (For AR exhibit)https://www.dbb.su.se/about-us/news/structure-reveals-new-routes-to-target-tuberculosis-1.416241