Photocobilins integrate B12 and bilin photochemistry for enzyme control

Shaowei Zhang (), Laura N. Jeffreys, Harshwardhan Poddar, Yuqi Yu, Chuanyang Liu, Kaylee Patel, Linus O. Johannissen, Lingyun Zhu, Matthew J. Cliff, Cunyu Yan, Giorgio Schirò, Martin Weik, Michiyo Sakuma, Colin W. Levy, David Leys, Derren J. Heyes () and Nigel S. Scrutton ()
Additional contact information
Shaowei Zhang: The University of Manchester
Laura N. Jeffreys: The University of Manchester
Harshwardhan Poddar: The University of Manchester
Yuqi Yu: The University of Manchester
Chuanyang Liu: National University of Defense Technology
Kaylee Patel: The University of Manchester
Linus O. Johannissen: The University of Manchester
Lingyun Zhu: National University of Defense Technology
Matthew J. Cliff: The University of Manchester
Cunyu Yan: The University of Manchester
Giorgio Schirò: Institut de Biologie Structurale
Martin Weik: Institut de Biologie Structurale
Michiyo Sakuma: The University of Manchester
Colin W. Levy: The University of Manchester
David Leys: The University of Manchester
Derren J. Heyes: The University of Manchester
Nigel S. Scrutton: The University of Manchester

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: Abstract Photoreceptor proteins utilise chromophores to sense light and trigger a biological response. The discovery that adenosylcobalamin (or coenzyme B12) can act as a light-sensing chromophore heralded a new field of B12-photobiology. Although microbial genome analysis indicates that photoactive B12-binding domains form part of more complex protein architectures, regulating a range of molecular–cellular functions in response to light, experimental evidence is lacking. Here we identify and characterise a sub-family of multi-centre photoreceptors, termed photocobilins, that use B12 and biliverdin (BV) to sense light across the visible spectrum. Crystal structures reveal close juxtaposition of the B12 and BV chromophores, an arrangement that facilitates optical coupling. Light-triggered conversion of the B12 affects quaternary structure, in turn leading to light-activation of associated enzyme domains. The apparent widespread nature of photocobilins implies involvement in light regulation of a wider array of biochemical processes, and thus expands the scope for B12 photobiology. Their characterisation provides inspiration for the design of broad-spectrum optogenetic tools and next generation bio-photocatalysts.

Date: 2024
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DOI: 10.1038/s41467-024-46995-1

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