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  • Perspective
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Bracing copper for the catalytic oxidation of C–H bonds

Nature Catalysis volume 1, pages 571–577 (2018)Cite this article

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Abstract

A structural unit found in the active site of some copper proteins, the histidine brace, is comprised of an N-terminal histidine that chelates a single copper ion through its amino terminus NH2 and the π–N of its imidazole side chain. Coordination is completed by the τ-N of a further histidine side chain, to give an overall N3 T-shaped coordination at the copper ion. The histidine brace appears in several proteins, including lytic polysaccharide monooxygenases LPMOs and particulate methane monooxygenases pMMOs, both of which catalyse the oxidation of substrates with strong C–H bonds (bond dissociation enthalpies ~100 kcal mol–1). As such, the copper histidine brace is the focus of research aimed at understanding how nature catalyses the oxidation of unactivated C–H bonds. In this Perspective, we evaluate these studies, which further give bioinspired direction to coordination chemists in the design and preparation of small molecule copper oxidation catalysts.

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Fig. 1: The copper histidine brace.
Fig. 2: LPMO active sites.
Fig. 3: The changing structure of the active site of pMMO.
Fig. 4: Deprotonation of the amino terminus.

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Acknowledgements

W.B.T. thanks the US National Institute of Health (grant R37GM47365) for financial support. L.C., G.J.D. and P.H.W. gratefully acknowledge the support of the UK’s Biotechnology and Biological Sciences Research Council (BBSRC) through grants BB/L001926/1 and BB/L021633/1. G.J.D. is a Royal Society Ken Murray Research Professor.

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Authors and Affiliations

  1. Department of Chemistry, University of York, Heslington, York, UK

    Luisa Ciano, Gideon J. Davies & Paul H. Walton

  2. Department of Chemistry, One Brookings Hall, Washington University in St. Louis, St. Louis, MO, USA

    William B. Tolman

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  1. Luisa Ciano
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  2. Gideon J. Davies
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  3. William B. Tolman
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Contributions

W.B.T. and P.H.W. wrote the manuscript, G.J.D. analysed LPMO and pMMO. protein structures and contributed to the writing of the manuscript. L.C. prepared metrical data for structure analysis and contributed to the writing of the manuscript.

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Correspondence to William B. Tolman or Paul H. Walton.

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Supplementary information

Supplementary Information

Supplementary Tables 1–3

Supplementary Data Set 1

Data from Supplementary Table 1: Collective metrics for copper histidine brace active site in known LPMO structures

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Ciano, L., Davies, G.J., Tolman, W.B. et al. Bracing copper for the catalytic oxidation of C–H bonds. Nat Catal 1, 571–577 (2018). https://doi.org/10.1038/s41929-018-0110-9

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