Spin crossover dynamics studies on the thermally activated molecular oxygen binding mechanism on a model copper complex-Reference-Cited by-同舟云学术

Spin crossover dynamics studies on the thermally activated molecular oxygen binding mechanism on a model copper complex

Published:2018 Issue:23 Volume:20 Page:15852-15862
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Bie Lihua¹²³⁴⁵,Liu Fang¹²³⁴⁵^ORCID,Li Yanwei⁶⁷⁸⁵,Dong Tiange¹²³⁴⁵,Gao Jun¹²³⁴⁵^ORCID,Du Likai¹²³⁴⁵^ORCID,Yuan Qiaoxia⁹³¹⁰⁵

Affiliation:

1. Hubei Key Laboratory of Agricultural Bioinformatics

2. College of Informatics

3. Huazhong Agricultural University

4. Wuhan

5. P. R. China

6. Environment Research Institute

7. Shandong University

8. Jinan

9. College of Engineering

10. Wuhan 430070

Abstract

The theoretical description of the primary dioxygen (O₂) binding and activation step in many copper or iron enzymes, suffers from the instrinsically electronic non-adiabaticity of the spin flip events of the triplet dioxygen molecule (³O₂), mediated by spin–orbit couplings.

Funder

National Natural Science Foundation of China

Huazhong Agricultural University

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C8CP02482K

Reference84 articles.

1. Reactivity of Dioxygen−Copper Systems

2. Recent Advances in Transition Metal Catalyzed Oxidation of Organic Substrates with Molecular Oxygen

3. Reduction of dioxygen by enzymes containing copper

4. Mononuclear copper active-oxygen complexes

5. The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation

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