Nonadiabatic Transition State Theory: Application to Intersystem Crossings in the Active Sites of Metal-Sulfur Proteins
DOI:
10.1002/qua.25124URI (для ссылок/цитирований):
https://elib.sfu-kras.ru/handle/2311/33251Автор:
Lykhin, A. O.
Kaliakin, D. G.
Depolo, E. S.
Kuzubov, A. A.
Varganov, S. A.
Коллективный автор:
Институт цветных металлов и материаловедения
Кафедра физической и неорганической химии
Дата:
2016Журнал:
International Journal of Quantum ChemistryКвартиль журнала в Scopus:
Q2Квартиль журнала в Web of Science:
Q1Библиографическое описание:
Lykhin, A. O. Nonadiabatic Transition State Theory: Application to Intersystem Crossings in the Active Sites of Metal-Sulfur Proteins [Текст] / A. O. Lykhin, D. G. Kaliakin, E. S. Depolo, A. A. Kuzubov, S. A. Varganov // International Journal of Quantum Chemistry. — 2016. — Т. 116. — С. 750-761Текст статьи не публикуется в открытом доступе в соответствии с политикой журнала.
Аннотация:
Nonadiabatic transition state theory (NA-TST) is a powerful tool
to investigate the nonradiative transitions between electronic
states with different spin multiplicities. The statistical nature of
NA-TST provides an elegant and computationally inexpensive
way to calculate the rate constants for intersystem crossings,
spin-forbidden reactions, and spin-crossovers in large complex
systems. The relations between the microcanonical and canoni-
cal versions of NA-TST and the traditional transition state theory
are shown, followed by a review of the basic steps in a typical
NA-TST rate constant calculation. These steps include evalua-
tions of the transition probability and coupling between electronic
states with different spin multiplicities, a search for the
minimum energy crossing point (MECP), and computing the
densities of states and partition functions for the reactant and
MECP structures. The shortcomings of the spin-diabatic version
of NA-TST related to ill-defined state coupling and state count-
ing are highlighted. In three examples, we demonstrate the
application of NA-TST to intersystem crossings in the active sites
of metal-sulfur proteins focusing on [NiFe]-hydrogenase, rubre-
doxin, and Fe2S2-ferredoxin. 2016 Wiley Periodicals, Inc.