A Catalytic Binding Site Together with a Distal Tyr in Myoglobin Affords Catalytic Efficiencies Similar to Natural Peroxidases-Reference-Cited by-同舟云学术

A Catalytic Binding Site Together with a Distal Tyr in Myoglobin Affords Catalytic Efficiencies Similar to Natural Peroxidases

Published:2019-12-19 Issue:1 Volume:10 Page:891-896
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Zhang Ping¹,Yuan Hong²,Xu Jiakun³,Wang Xiao-Juan¹,Gao Shu-Qin⁴,Tan Xiangshi²,Lin Ying-Wu¹⁴^ORCID

Affiliation:

1. School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China

2. Department of Chemistry & Institute of Biomedical Science, Fudan University, Shanghai 200433, China

3. Key Lab of Sustainable Development of Polar Fisheries, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China

4. Lab of Protein Structure and Function, University of South China, Hengyang 421001, China

Funder

National Natural Science Foundation of China

Ministry of Agriculture and Rural Affairs of the People's Republic of China

Human Provincial Innovation Foundation for Postgraduate

Special Scientific Research Funds for Central Nonprofit Institutes, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.9b05080

Reference39 articles.

1. Design of functional metalloproteins

2. Rational design of metalloenzymes: From single to multiple active sites

3. Hemoproteins Reconstituted with Artificial Metal Complexes as Biohybrid Catalysts

4. Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors

5. A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme

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