Electronic coupling in a synthetic model of the Cu–cofactor unit of the PM state in cytochrome c oxidase

Sang Tae Lee; Christopher G. Bailey; Daniel A. Santos; Mohan Bhadbhade; Heejin Kim; Dong Jun Kim

doi:10.1039/D5CC05355B

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Electronic coupling in a synthetic model of the Cu–cofactor unit of the P_M state in cytochrome c oxidase

Sang Tae Lee,

^a Christopher G. Bailey,

^bc Daniel A. Santos,

^a Mohan Bhadbhade,

^d Heejin Kim

*^e and Dong Jun Kim

*^a

Author affiliations

* Corresponding authors

^a School of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia
E-mail: dongjun.kim@unsw.edu.au

^b School of Physics, The University of Sydney, Sydney, NSW 2006, Australia

^c Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia

^d Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052, Australia

^e Research Center for Materials Analysis, Korea Basic Science Institute, Daejeon 34133, Republic of Korea
E-mail: heejinkim@kbsi.re.kr

Abstract

A hydroquinone–imidazole–Cu(II) complex reproduces the Tyr–His–Cu unit of cytochrome c oxidase. Laser-induced EPR and DFT reveal a semiquinone radical electronically isolated from Cu(II) by orthogonal orbital alignment. The weak magnetic exchange underscores how geometry governs coupling, providing insight into transient states of metalloenzymes and their synthetic analogues.

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DOI: https://doi.org/10.1039/D5CC05355B
Article type: Communication
Submitted: 17 Sep 2025
Accepted: 31 Dec 2025
First published: 03 Jan 2026
This article is Open Access

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Chem. Commun., 2026,62, 2986-2990

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Electronic coupling in a synthetic model of the Cu–cofactor unit of the P_M state in cytochrome c oxidase

S. T. Lee, C. G. Bailey, D. A. Santos, M. Bhadbhade, H. Kim and D. J. Kim, Chem. Commun., 2026, 62, 2986 DOI: 10.1039/D5CC05355B

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Chemical Communications

Electronic coupling in a synthetic model of the Cu–cofactor unit of the P_M state in cytochrome c oxidase

Abstract

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Electronic coupling in a synthetic model of the Cu–cofactor unit of the P_M state in cytochrome c oxidase

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