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Photocobilins integrate B 12 and bilin photochemistry for enzyme control.
- Source :
-
Nature communications [Nat Commun] 2024 Mar 28; Vol. 15 (1), pp. 2740. Date of Electronic Publication: 2024 Mar 28. - Publication Year :
- 2024
-
Abstract
- Photoreceptor proteins utilise chromophores to sense light and trigger a biological response. The discovery that adenosylcobalamin (or coenzyme B <subscript>12</subscript> ) can act as a light-sensing chromophore heralded a new field of B <subscript>12</subscript> -photobiology. Although microbial genome analysis indicates that photoactive B <subscript>12</subscript> -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 <subscript>12</subscript> and biliverdin (BV) to sense light across the visible spectrum. Crystal structures reveal close juxtaposition of the B <subscript>12</subscript> and BV chromophores, an arrangement that facilitates optical coupling. Light-triggered conversion of the B <subscript>12</subscript> 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 <subscript>12</subscript> photobiology. Their characterisation provides inspiration for the design of broad-spectrum optogenetic tools and next generation bio-photocatalysts.<br /> (© 2024. The Author(s).)
Details
- Language :
- English
- ISSN :
- 2041-1723
- Volume :
- 15
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Nature communications
- Publication Type :
- Academic Journal
- Accession number :
- 38548733
- Full Text :
- https://doi.org/10.1038/s41467-024-46995-1