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Metalloproteins

A switch for blue copper proteins?

Nature Chemistry volume 8, pages 639–641 (2016)Cite this article

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Nitric oxide (NO) has important functions in all forms of life and serves, for example, as a signalling molecule in mammals. Now, two complementary studies have uncovered how NO binds to blue copper proteins. This research suggests a mechanism by which NO could regulate the activity of blue copper proteins involved in denitrification.

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Figure 1: Reaction of NO with blue copper centres.
Figure 2: Reversible formation of an S–nitrosothiol adduct.

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References

  1. Moncada, S., Palmer, R. M. & Higgs, E. A. Pharmacol. Rev. 43, 109–142 (1991).

    CAS  PubMed  Google Scholar 

  2. Snyder, S. H. Science 257, 494–496 (1992).

    Article  CAS  Google Scholar 

  3. Lehnert, N., Berto, T. C., Galinato, M. G. I. & Goodrich, L. E. in The Handbook of Porphyrin Science Vol. 14 (eds Kadish, K. M. et al.) 1–247 (World Scientific, 2011).

    Google Scholar 

  4. Richardson, D. J. & Watmough, N. J. Curr. Opin. Chem. Biol. 3, 207–219 (1999).

    Article  CAS  Google Scholar 

  5. Cary, S. P. L., Winger, J. A., Derbyshire, E. R. & Marletta, M. A. Trends Biochem. Sci. 31, 231–239 (2006).

    Article  CAS  Google Scholar 

  6. Hunt, A. P. & Lehnert, N. Acc. Chem. Res. 48, 2117–2125 (2015).

    Article  CAS  Google Scholar 

  7. Gardner, A. M., Helmick, R. A. & Gardner, P. R. J. Biol. Chem. 277, 8172–8177 (2002).

    Article  CAS  Google Scholar 

  8. Ding, H. & Demple, B. Proc. Natl Acad. Sci. USA 97, 5146–5150 (2000).

    Article  CAS  Google Scholar 

  9. D'Autréaux, B., Tucker, N. P., Dixon, R. & Spiro, S. Nature 437, 769–772 (2005).

    Article  Google Scholar 

  10. Merkle, A. C. & Lehnert, N. Dalton Trans. 41, 3355–3368 (2012).

    Article  CAS  Google Scholar 

  11. Solomon, E. I. Inorg. Chem. 45, 8012–8025 (2006).

    Article  CAS  Google Scholar 

  12. Gorren, A. C. F., de Boer, E. & Wever, R. Biochim. Biophys. Acta 916, 38–47 (1987).

    Article  CAS  Google Scholar 

  13. Zhang, S., Melzer, M. M., Sen, S. N., Çelebi-Ölçüm, N. & Warren, T. H. Nature Chem. 8, 663–669 (2016).

    Article  CAS  Google Scholar 

  14. Tian, S. et al. Nature Chem. 8, 670–677 (2016).

    Article  CAS  Google Scholar 

Download references

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Authors and Affiliations

  1. Subhra Samanta and Nicolai Lehnert are in the Department of Chemistry and Department of Biophysics, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109, USA,

    Subhra Samanta & Nicolai Lehnert

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  1. Subhra Samanta
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  2. Nicolai Lehnert
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Correspondence to Nicolai Lehnert.

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Samanta, S., Lehnert, N. A switch for blue copper proteins?. Nature Chem 8, 639–641 (2016). https://doi.org/10.1038/nchem.2561

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