A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome.

ABSTRACT: An animal-like cryptochrome derived from Chlamydomonas reinhardtii (CraCRY) is a bifunctional flavoenzyme harboring flavin adenine dinucleotide (FAD) as a photoreceptive/catalytic center and functions both in the regulation of gene transcription and the repair of UV-induced DNA lesions in a light-dependent manner, using different FAD redox states. To address how CraCRY stabilizes the physiologically relevant redox state of FAD, we investigated the thermodynamic and kinetic stability of the two-electron reduced anionic FAD state (FADH^-) in CraCRY and related (6-4) photolyases. The thermodynamic stability of FADH^- remained almost the same compared to that of all tested proteins. However, the kinetic stability of FADH^- varied remarkably depending on the local

SUBMITTER: Hosokawa Y 

PROVIDER: S-EPMC10551024 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature