Redox driven B12-ligand switch drives CarH photoresponse
Harshwardhan Poddar,
Ronald Rios-Santacruz,
Derren J. Heyes,
Muralidharan Shanmugam,
Adam Brookfield,
Linus O. Johannissen,
Colin W. Levy,
Laura N. Jeffreys,
Shaowei Zhang,
Michiyo Sakuma,
Jacques-Philippe Colletier,
Sam Hay,
Giorgio Schirò,
Martin Weik,
Nigel S. Scrutton () and
David Leys ()
Additional contact information
Harshwardhan Poddar: University of Manchester
Ronald Rios-Santacruz: Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
Derren J. Heyes: University of Manchester
Muralidharan Shanmugam: University of Manchester
Adam Brookfield: University of Manchester
Linus O. Johannissen: University of Manchester
Colin W. Levy: University of Manchester
Laura N. Jeffreys: University of Manchester
Shaowei Zhang: University of Manchester
Michiyo Sakuma: University of Manchester
Jacques-Philippe Colletier: Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
Sam Hay: University of Manchester
Giorgio Schirò: Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
Martin Weik: Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
Nigel S. Scrutton: University of Manchester
David Leys: University of Manchester
Nature Communications, 2023, vol. 14, issue 1, 1-14
Abstract:
Abstract CarH is a coenzyme B12-dependent photoreceptor involved in regulating carotenoid biosynthesis. How light-triggered cleavage of the B12 Co-C bond culminates in CarH tetramer dissociation to initiate transcription remains unclear. Here, a series of crystal structures of the CarH B12-binding domain after illumination suggest formation of unforeseen intermediate states prior to tetramer dissociation. Unexpectedly, in the absence of oxygen, Co-C bond cleavage is followed by reorientation of the corrin ring and a switch from a lower to upper histidine-Co ligation, corresponding to a pentacoordinate state. Under aerobic conditions, rapid flash-cooling of crystals prior to deterioration upon illumination confirm a similar B12-ligand switch occurs. Removal of the upper His-ligating residue prevents monomer formation upon illumination. Combined with detailed solution spectroscopy and computational studies, these data demonstrate the CarH photoresponse integrates B12 photo- and redox-chemistry to drive large-scale conformational changes through stepwise Co-ligation changes.
Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40817-6
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DOI: 10.1038/s41467-023-40817-6
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