Borodulin RR, Dereven’kov IA, Burbaev DS, Makarov SV, Mikoyan VD, Serezhenkov VА, Kubrina LN, Ivanovic-Burmazovic I, Vanin AF (2014)
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2014
Book Volume: 40
Pages Range: 100-109
DOI: 10.1016/j.niox.2014.06.005
EPR, optical, electrochemical and stopped-flow methods were used to demonstrate that Fe(NO) fragments in paramagnetic mononuclear and diamagnetic binuclear forms of dinitrosyl iron complexes with glutathione are reversibly reduced by a two-electron mechanism to be further transformed from the initial state with d configuration into states with the d and d electronic configurations of the iron atom. Under these conditions, both forms of DNIC display identical optical and EPR characteristics in state d suggesting that reduction of the binuclear form of DNIC initiates their reversible decomposition into two mononuclear dinitrosyl iron fragments, one of which is EPR-silent (d ) and the other one is EPR-active (d). Both forms of DNIC produce EPR signals with the following values of the g-factor: g = 2.01, g = 1.97, g = 2.0. M-DNIC with glutathione manifest an ability to pass into state d, however, only in solutions with a low content of free glutathione. Similar transitions were established for protein-bound M- and B-DNIC with thiol-containing ligands. © 2014 Elsevier Ltd. All rights reserved.
APA:
Borodulin, R.R., Dereven’kov, I.A., Burbaev, D.S., Makarov, S.V., Mikoyan, V.D., Serezhenkov, V.А.,... Vanin, A.F. (2014). Redox activities of mono- and binuclear forms of low-molecular and protein-bound dinitrosyl iron complexes with thiol-containing ligands. Nitric Oxide - Biology and Chemistry, 40, 100-109. https://doi.org/10.1016/j.niox.2014.06.005
MLA:
Borodulin, Rostislav R., et al. "Redox activities of mono- and binuclear forms of low-molecular and protein-bound dinitrosyl iron complexes with thiol-containing ligands." Nitric Oxide - Biology and Chemistry 40 (2014): 100-109.
BibTeX: Download