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It consists of a copper ion chelated by the NH\n                    <jats:sub>2<\/jats:sub>\n                    and \u03c0\u2010N atom of an N\u2010terminal histidine, and the \u03c4\u2010N atom of a further histidine, in an overall T\u2010shaped coordination geometry (\n                    <jats:italic>Nat Catal<\/jats:italic>\n                    2018,\n                    <jats:bold>1<\/jats:bold>\n                    , 571). Like haem\u2010containing proteins, histidine\u2010brace\u2010containing proteins have peroxygenase and\/or oxygenase activity, where the substrates are notable for resistance to oxidation, for example, lytic polysaccharide monooxygenases (LPMOs). Moreover, the histidine brace is an invariant unit around which different protein structures exert different activities. Given the similarities in the diversity of function of proteins that contain either the copper histidine brace or haem,\n                    <jats:italic>the question arises as to whether the functions of histidine brace\u2010containing proteins duplicate those containing haem groups.<\/jats:italic>\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.14579","type":"journal-article","created":{"date-parts":[[2023,1,20]],"date-time":"2023-01-20T03:43:24Z","timestamp":1674186204000},"page":"485-494","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["The histidine brace: nature's copper alternative to haem?"],"prefix":"10.1002","volume":"597","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1152-1480","authenticated-orcid":false,"given":"Paul H.","family":"Walton","sequence":"first","affiliation":[{"name":"Department of Chemistry University of York  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