Investigating radical pair reaction dynamics of B 12 coenzymes 2: Time-resolved electron paramagnetic resonance spectroscopy.

Autor: Lukinović V; Institute of Biochemistry, Carleton University, Ottawa, Ontario, Canada., Hughes JA; Laboratory of Ultrafast Spectroscopy, ISIC, and Lausanne Centre for Ultrafast Science (LACUS), École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland., Woodward JR; Graduate School of Arts and Sciences, The University of Tokyo, Tokyo, Japan., Jones AR; Biometrology, Department of Chemical and Biological Sciences, National Physical Laboratory, Middlesex, United Kingdom. Electronic address: alex.jones@npl.co.uk.
Jazyk: angličtina
Zdroj: Methods in enzymology [Methods Enzymol] 2022; Vol. 669, pp. 283-301. Date of Electronic Publication: 2022 Jan 29.
DOI: 10.1016/bs.mie.2021.12.020
Abstrakt: The chemistry of B 12 coenzymes is highly sensitive to the nature of their upper axial ligand and can be further tuned by their environment. Methylcobalamin, for example, generates RPs photochemically but undergoes non-radical biochemistry when bound to its dependent enzymes. Owing to the transient nature of the reaction intermediates, it remains a challenge to investigate how their environment controls reactivity. Here, we describe how to use time-resolved electron paramagnetic spectroscopy to directly monitor the generation and evolution of transient radicals that result from the photolysis of a B 12 coenzyme. This method produces evolving, spin-polarized spectra that are rich in mechanistic detail.
(Copyright © 2022 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: