Abstract
The aerobic respiratory chain of Escherichia coli has two terminal quinol oxidases: cytochrome bo and cytochrome bd. Cytochrome bd was thought to function solely to facilitate micro-aerobic respiration. However, it has recently been shown to be overexpressed under conditions of nitric oxide (NO) stress; we show here that cytochrome bd is crucial for protecting E. coli cells from NO-induced growth inhibition by virtue of its fast NO dissociation rate.
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Acknowledgements
We thank the Wellcome Trust (069769) and the Biotechnology and Biological Sciences Research Council (BB/D017858/1) for financial support.
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M.G.M., P.S.D. and C.E.C. designed the experiments; M.G.M., M.S. and K.S.D. performed the experiments; M.G.M., M.S., P.N., K.S.D., R.K.P. and C.E.C. analyzed the data; and M.G.M., M.S., R.K.P. and C.E.C. wrote the paper.
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Mason, M., Shepherd, M., Nicholls, P. et al. Cytochrome bd confers nitric oxide resistance to Escherichia coli. Nat Chem Biol 5, 94–96 (2009). https://doi.org/10.1038/nchembio.135
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DOI: https://doi.org/10.1038/nchembio.135
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