Coenzyme B12 binding proteins have gained a lot of attention recently for their ability to respond to light and act as photoreceptors.1 CarH is a bacterial coenzyme B12-dependent photoreceptor involved in regulating the expression of carotenoid biosynthetic genes.1 In the dark, CarH is a tetramer and suppresses transcription by binding to the promoter region. Upon illumination of CarH, the photosensitive Co-C bond in B12 is cleaved, triggering a series of intermediate states which culminates in the light-adapted, monomer formation and release of DNA. The nature of the Co-C bond cleavage (homolytic vs heterolytic) and the different intermediates formed during the photocycle remains poorly characterized.2-4
In this presentation the crystal structures of the native and photo-activated CarH from Thermus thermophilus, TtCBD enzyme and the associated dynamics of the B12-chromophore during the photocatalysis will be discussed.5 The cryo-trapping experiment along with cw-EPR/annealing and spin-trapping techniques revealing the possible intermediates present along the CarH photocycle. The role of the axial H132 ligand in the photocycle and the UV-Vis data of these enzymes will also be discussed in detail.
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