The interplay between chromophore and protein determines the extended excited state dynamics in a single-domain phytochrome.

ABSTRACT: Phytochromes are a diverse family of bilin-binding photoreceptors that regulate a wide range of physiological processes. Their photochemical properties make them attractive for applications in optogenetics and superresolution microscopy. Phytochromes undergo reversible photoconversion triggered by the Z ⇄ E photoisomerization about the double bond in the bilin chromophore. However, it is not fully understood at the molecular level how the protein framework facilitates the complex photoisomerization dynamics. We have studied a single-domain bilin-binding photoreceptor All2699g1 (Nostoc sp. PCC 7120) that exhibits photoconversion between the red light-absorbing (P_r) and far red-absorbing (P_fr) states just like canonical phytochromes. We present the

SUBMITTER: Slavov C 

PROVIDER: S-EPMC7368379 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature