Set of Fe(II)-3-Hydroxyflavonolate Enzyme–Substrate Model Complexes of Atypically Coordinated Mononuclear Non-Heme Fe(II)-Dependent Quercetin 2,4-Dioxygenase-Reference-Cited by-同舟云学术

Set of Fe(II)-3-Hydroxyflavonolate Enzyme–Substrate Model Complexes of Atypically Coordinated Mononuclear Non-Heme Fe(II)-Dependent Quercetin 2,4-Dioxygenase

Published:2017-09-18 Issue:9 Volume:2 Page:5850-5860
ISSN:2470-1343
Container-title:ACS Omega
language:en
Short-container-title:ACS Omega

Author:

Sun Ying-Ji¹^ORCID,Huang Qian-Qian¹,Zhang Jian-Jun¹

Affiliation:

1. School of Chemistry, Dalian University of Technology, 2 Linggong Road, Dalian 116024, China

Funder

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acsomega.7b00927

Reference42 articles.

1. Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites

2. A novel β-diketone-cleaving enzyme from Acinetobacter johnsonii: acetylacetone 2,3-oxygenase

3. Structure and mechanism of mouse cysteine dioxygenase

4. One Protein, Two Enzymes Revisited: A Structural Entropy Switch Interconverts the Two Isoforms of Acireductone Dioxygenase

5. The Crystal Structure of a Quercetin 2,3-Dioxygenase from Bacillus subtilis Suggests Modulation of Enzyme Activity by a Change in the Metal Ion at the Active Site(s)

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