On the Role of the Conserved Histidine at the Chromophore Isomerization Site in Phytochromes.
Journal
The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530
Informations de publication
Date de publication:
23 12 2021
23 12 2021
Historique:
pubmed:
30
11
2021
medline:
27
1
2022
entrez:
29
11
2021
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 34843240
doi: 10.1021/acs.jpcb.1c08245
pmc: PMC9447488
mid: NIHMS1833506
doi:
Substances chimiques
Bacterial Proteins
0
Tetrapyrroles
0
Phytochrome
11121-56-5
Histidine
4QD397987E
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
13696-13709Subventions
Organisme : NIGMS NIH HHS
ID : T34 GM105549
Pays : United States
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