Unraveling the Photoactivation Mechanism of a Light-Activated Adenylyl Cyclase Using Ultrafast Spectroscopy Coupled with Unnatural Amino Acid Mutagenesis.
Journal
ACS chemical biology
ISSN: 1554-8937
Titre abrégé: ACS Chem Biol
Pays: United States
ID NLM: 101282906
Informations de publication
Date de publication:
16 09 2022
16 09 2022
Historique:
pubmed:
30
8
2022
medline:
20
9
2022
entrez:
29
8
2022
Statut:
ppublish
Résumé
The hydrogen bonding network that surrounds the flavin in blue light using flavin adenine dinucleotide (BLUF) photoreceptors plays a crucial role in sensing and communicating the changes in the electronic structure of the flavin to the protein matrix upon light absorption. Using time-resolved infrared spectroscopy (TRIR) and unnatural amino acid incorporation, we investigated the photoactivation mechanism and the role of the conserved tyrosine (Y6) in the forward reaction of the photoactivated adenylyl cyclase from
Identifiants
pubmed: 36038143
doi: 10.1021/acschembio.2c00575
pmc: PMC9486806
doi:
Substances chimiques
Amino Acids
0
Bacterial Proteins
0
Flavins
0
Protons
0
Flavin-Adenine Dinucleotide
146-14-5
Tyrosine
42HK56048U
Adenosine Triphosphate
8L70Q75FXE
Adenylyl Cyclases
EC 4.6.1.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
2643-2654Subventions
Organisme : NIGMS NIH HHS
ID : K12 GM102778
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM092714
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM135746
Pays : United States
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