On the Role of the Conserved Histidine at the Chromophore Isomerization Site in Phytochromes.

ABSTRACT: Phytochromes are sensory photoreceptors that use light to drive protein structural changes, which in turn trigger physiological reaction cascades. The process starts with a double-bond photoisomerization of the linear methine-bridged tetrapyrrole chromophore in the photosensory core module. The molecular mechanism of the photoconversion depends on the structural and electrostatic properties of the chromophore environment, which are highly conserved in related phytochromes. However, the specific role of individual amino acids is yet not clear. A histidine in the vicinity of the isomerization site is highly conserved and almost invariant among all phytochromes. The present study aimed at analyzing its role by taking advantage of a myxobacterial phytochrome SaBphP1 from Stigmatella auranti

SUBMITTER: Kraskov A 

PROVIDER: S-EPMC9447488 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature