Dioxygen Activation by Iron Complexes: The Catalytic Role of Intersystem Crossing Dynamics for a Heme-Related Model

Likai Du*, Fang Liu, Yanwei Li, Zhongyue Yang, Qingzhu Zhang, Chaoyuan Zhu, Jun Gao

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Enzymes containing heme, nonheme iron, or copper active sites play an essential role in the dioxygen binding and activation for substrate oxidation. The conceptual challenges to the quantitative modeling of this primary catalytic step arise from (1) instrinsic electronic nonadiabaticity of the spin flip events of the triplet dioxygen molecule (3O2), mediated by spin-orbit coupling and (2) possible heat dissipation channels, due to the high exothermicity of dioxygen binding processes. Herein, the spin-forbidden dioxygen binding dynamics of a reduced heme model was directly investigated in terms of the nonadiabatic trajectory surface-hopping dynamics, involving the coupled singlet, triplet and quintet states. This work reveals the complexity of this elemental reaction, and the binding/dissociation dynamics of iron peroxo species is important to interpret the subsequent H atom abstraction reaction step. Furthermore, we identify nonadiabatic dynamical effects that could not be observed through traditional calculations of static geometries.

Original languageEnglish
Pages (from-to)2821-2831
Number of pages11
JournalJournal of Physical Chemistry C
Volume122
Issue number5
DOIs
StatePublished - 8 Feb 2018

Fingerprint Dive into the research topics of 'Dioxygen Activation by Iron Complexes: The Catalytic Role of Intersystem Crossing Dynamics for a Heme-Related Model'. Together they form a unique fingerprint.

Cite this