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Cited by 13Photoreceptor and optogenetics researchPorphyrin Metabolism and DisordersMetalloenzymes and iron-sulfur proteins

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Photocobilins integrate B12 and bilin photochemistry for enzyme control

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Zhang, Shaowei, Jeffreys, Laura N., Poddar, Harshwardhan, Yu, Yuqi, Liu, Chuanyang, Patel, Kaylee, Johannissen, Linus O., Zhu, Lingyun, Cliff, Matthew J., Yan, Cunyu, Schirò, Giorgio, Weik, Martin, Sakuma, Michiyo, Levy, Colin W., Leys, David, Heyes, Derren J., Scrutton, Nigel S.·2024·Nature Communications
DOI 10.1038/s41467-024-46995-1PMC PMC10979010

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Abstract

Photoreceptor proteins utilise chromophores to sense light and trigger a biological response. The discovery that adenosylcobalamin (or coenzyme B 12 ) can act as a light-sensing chromophore heralded a new field of B 12 -photobiology. Although microbial genome analysis indicates that photoactive B 12 -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 B 12 and biliverdin (BV) to sense light across the visible spectrum. Crystal structures reveal close juxtaposition of the B 12 and BV chromophores, an arrangement that facilitates optical coupling. Light-triggered conversion of the B 12 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 B 12 photobiology. Their characterisation provides inspiration for the design of broad-spectrum optogenetic tools and next generation bio-photocatalysts.

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Metadata

Authors
Zhang, S., Jeffreys, L. N., Poddar, H., Yu, Y., Liu, C., Patel, K., Johannissen, L. O., Zhu, L., Cliff, M. J., Yan, C., Schirò, G., Weik, M., Sakuma, M., Levy, C. W., Leys, D., Heyes, D. J., & Scrutton, N. S.
Affiliations
  • National University of Defense Technology (CN)
  • University of Manchester (GB)
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
  • Zhang, Shaowei
  • Heyes, Derren J.
  • Scrutton, Nigel S.
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2024-03-28
Volume
15
Issue
1
Pages
2740-2740
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-024-46995-1
PMC
PMC10979010
OpenAlex
W4393280358
Cited by
13
References
1
Citations by year
2026: 5 · 2025: 5 · 2024: 3
FWCI
2.27
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Research Square (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research Explorer (The University of Manchester) (publishedVersion, cc-by)
  • HAL (submittedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • RCUK | Engineering and Physical Sciences Research Council (EP/S030336/1)
  • NUDT | Science and Technology on Advanced Ceramic Fibers and Composites Laboratory (22-ZZCX-039, 22-02-15)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Keywords
adenosylcobalamin, coenzyme B12, biliverdin, quaternary structure, optogenetics, crystal structure
MeSH terms
Bacterial Proteins, Bile Pigments, Biliverdine, Light, Photochemistry, Photoreceptors, Microbial

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