Identification of the vibrational marker of tyrosine cation radical using ultrafast transient infrared spectroscopy of flavoprotein systems

Autor: James N. Iuliano, Peter J. Tonge, Ildiko Pecsi, Ursula Liebl, Lipsa Nag, Jinnette Tolentino Collado, Stephen R. Meech, Gregory M. Greetham, Ian P. Clark, Zsuzsanna Fekete, Pierre Sournia, Katalin Pirisi, Andras Lukacs, Marten H. Vos
Přispěvatelé: Vos, Marten, University of Pécs Medical School (UP MS), University of Pecs, Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Department of Chemistry (Stony Brook, USA, Stony Brook University [SUNY] (SBU), State University of New York (SUNY)-State University of New York (SUNY), Central Laser Facility (CLF), STFC Rutherford Appleton Laboratory (RAL), Science and Technology Facilities Council (STFC)-Science and Technology Facilities Council (STFC), University of East Anglia [Norwich] (UEA), School of Chemistry, University of East Anglia
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: Photochem Photobiol Sci
Photochemical & Photobiological Sciences
Photochemical & Photobiological Sciences, 2021, ⟨10.1007/s43630-021-00024-y⟩
Photochemical & Photobiological Sciences, Royal Society of Chemistry, 2021, ⟨10.1007/s43630-021-00024-y⟩
ISSN: 1474-9092
1474-905X
DOI: 10.1007/s43630-021-00024-y⟩
Popis: 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.
Databáze: OpenAIRE