Identification of the vibrational marker of tyrosine cation radical using ultrafast transient infrared spectroscopy of flavoprotein systems.
Bacterial Proteins
/ chemistry
Cations
/ chemistry
Flavoproteins
/ chemistry
Free Radicals
/ chemistry
Glucose Oxidase
/ chemistry
Methyltransferases
/ chemistry
Mutagenesis, Site-Directed
Photosynthetic Reaction Center Complex Proteins
/ chemistry
Recombinant Proteins
/ biosynthesis
Rhodobacter sphaeroides
/ metabolism
Spectrophotometry, Infrared
Tyrosine
/ chemistry
Journal
Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
ISSN: 1474-9092
Titre abrégé: Photochem Photobiol Sci
Pays: England
ID NLM: 101124451
Informations de publication
Date de publication:
Mar 2021
Mar 2021
Historique:
received:
11
01
2021
accepted:
09
02
2021
pubmed:
16
3
2021
medline:
13
7
2021
entrez:
15
3
2021
Statut:
ppublish
Résumé
Tryptophan and tyrosine radical intermediates play crucial roles in many biological charge transfer processes. Particularly in flavoprotein photochemistry, short-lived reaction intermediates can be studied by the complementary techniques of ultrafast visible and infrared spectroscopy. The spectral properties of tryptophan radical are well established, and the formation of neutral tyrosine radicals has been observed in many biological processes. However, only recently, the formation of a cation tyrosine radical was observed by transient visible spectroscopy in a few systems. Here, we assigned the infrared vibrational markers of the cationic and neutral tyrosine radical at 1483 and 1502 cm
Identifiants
pubmed: 33721272
doi: 10.1007/s43630-021-00024-y
pii: 10.1007/s43630-021-00024-y
pmc: PMC8791523
mid: NIHMS1768152
doi:
Substances chimiques
Bacterial Proteins
0
Cations
0
Flavoproteins
0
Free Radicals
0
Photosynthetic Reaction Center Complex Proteins
0
Recombinant Proteins
0
tyrosine radical
0
Tyrosine
42HK56048U
Glucose Oxidase
EC 1.1.3.4
Methyltransferases
EC 2.1.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
369-378Subventions
Organisme : NKFIH
ID : NKFIH 2017-2.2.5-TÉT-FR-2017-00005
Organisme : NIGMS NIH HHS
ID : T32 GM092714
Pays : United States
Organisme : National Science Foundation
ID : MCB-1817837 to PJT
Organisme : Stony Brook University
ID : 5R25GM103962-04
Organisme : NIGMS NIH HHS
ID : R25 GM103962
Pays : United States
Organisme : CNRS
ID : PHC Balaton 40173VE
Organisme : Engineering and Physical Sciences Research Council
ID : EP/N033647/1
Organisme : EFOP
ID : EFOP-3.6.2-16-2017-00005
Organisme : Foundation for the National Institutes of Health
ID : T32GM092714)
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