Journal
PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES
Volume 20, Issue 3, Pages 369-378Publisher
SPRINGERNATURE
DOI: 10.1007/s43630-021-00024-y
Keywords
-
Funding
- University of Pecs
- EPSRC [EP/N033647/1] Funding Source: UKRI
Ask authors/readers for more resources
Tryptophan and tyrosine radical intermediates are crucial in biological charge transfer processes and can be studied using ultrafast visible and infrared spectroscopy. Recent studies have observed the formation of neutral tyrosine radicals in biological processes and, in a few systems, the formation of cation tyrosine radicals. Transient infrared spectroscopy shows sensitivity to specific radicals at low concentrations, as demonstrated in various studies.
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(-1) (in deuterated buffer), respectively, in a variant of the bacterial methyl transferase TrmFO, and in the native glucose oxidase. In addition, we studied a mutant of AppABLUF blue-light sensor domain from Rhodobacter sphaeroides in which only a direct formation of the neutral radical was observed. Our studies highlight the exquisite sensitivity of transient infrared spectroscopy to low concentrations of specific radicals.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available