Monophenolase and catecholase activity ofAspergillus oryzaecatechol oxidase: insights from hybrid QM/MM calculations-Reference-Cited by-同舟云学术

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Monophenolase and catecholase activity ofAspergillus oryzaecatechol oxidase: insights from hybrid QM/MM calculations

Published:2020 Issue:27 Volume:18 Page:5192-5202
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Jiang Hao¹²³⁴^ORCID,Lai Wenzhen¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. Renmin University of China

3. Beijing

4. China

Abstract

Monophenolase and diphenolase activities of the [Cu₂O₂]²⁺active site ofAspergillus oryzaecatechol oxidase are revealed by hybrid QM/MM calculations.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/OB/D0OB00969E

Reference85 articles.

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2. Oxidative CarbonCarbon Bond Cleavage of a α-Hydroxy Ketone by a Functional Model of 2,4′-Dihydroxyacetophenone Dioxygenase

3. Dioxygen Reactivity of Biomimetic Iron-Catecholate and Iron-o-Aminophenolate Complexes of a Tris(2-pyridylthio)methanido Ligand: Aromatic CC Bond Cleavage of Catecholate versuso-Iminobenzosemiquinonate Radical Formation

4. The Crystal Structure of Catechol Oxidase: New Insight into the Function of Type-3 Copper Proteins

5. What causes the different functionality in type-III-copper enzymes? A state of the art perspective

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