The histidine brace: nature's copper alternative to haem?

TY - JOUR

T1 - The histidine brace

T2 - nature's copper alternative to haem?

AU - Walton, Paul H.

AU - Davies, Gideon J.

AU - Diaz, Daniel E.

AU - Franco-Cairo, João P.

N1 - © 2023 The Authors. Funding Information: GJD and PHW thank the Biotechnology and Biological Sciences Research Council for support (BB/R007705/1, BB/V0040069/1).

PY - 2023/2/27

Y1 - 2023/2/27

N2 - The copper histidine brace is a structural unit in metalloproteins (Proc Natl Acad Sci USA 2011, 108, 15079). It consists of a copper ion chelated by the NH2 and π-N atom of an N-terminal histidine, and the τ-N atom of a further histidine, in an overall T-shaped coordination geometry (Nat Catal 2018, 1, 571). Like haem-containing proteins, histidine-brace-containing 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, the question arises as to whether the functions of histidine brace-containing proteins duplicate those containing haem groups.

AB - The copper histidine brace is a structural unit in metalloproteins (Proc Natl Acad Sci USA 2011, 108, 15079). It consists of a copper ion chelated by the NH2 and π-N atom of an N-terminal histidine, and the τ-N atom of a further histidine, in an overall T-shaped coordination geometry (Nat Catal 2018, 1, 571). Like haem-containing proteins, histidine-brace-containing 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, the question arises as to whether the functions of histidine brace-containing proteins duplicate those containing haem groups.

KW - copper

KW - haem

KW - histidine brace

KW - LPMOs

UR - http://www.scopus.com/inward/record.url?scp=85147343887&partnerID=8YFLogxK

U2 - 10.1002/1873-3468.14579

DO - 10.1002/1873-3468.14579

M3 - Review article

C2 - 36660911

AN - SCOPUS:85147343887

SN - 0014-5793

VL - 597

SP - 485

EP - 494

JO - FEBS Letters

JF - FEBS Letters

IS - 4

ER -