Design and engineering of an artificial disulfide bond in human cytochrome <i>c</i> to regulate the protein structure and function-Reference-Cited by-同舟云学术

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Design and engineering of an artificial disulfide bond in human cytochrome c to regulate the protein structure and function

Published:2024 Issue:6 Volume:9 Page:649-659
ISSN:2058-9689
Container-title:Molecular Systems Design & Engineering
language:en
Short-container-title:Mol. Syst. Des. Eng.

Author:

Li Yan-Yan¹,Feng Yu¹,Yu Lu²^ORCID,Long Shuang-Shuang¹,Gao Shu-Qin³,Lin Ying-Wu¹³^ORCID

Affiliation:

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

2. High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, China

3. Key Lab of Protein Structure and Function of Universities in Hunan Province, University of South China, Hengyang 421001, China

Abstract

An artificial disulfide bond was rationally constructed in human cytochrome c (hCyt c) via double mutations (A51C/G77C), which weakened the coordination of Met80 to the heme iron and enhanced the peroxidase activity of hCyt c.

Funder

National Natural Science Foundation of China

Natural Science Foundation of Hunan Province

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/ME/D3ME00196B

Reference62 articles.

1. Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins

2. Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers

3. Heme Enzyme Structure and Function

4. Carbon–fluorine bond cleavage mediated by metalloenzymes

5. Cytochrome c: Occurrence and Functions

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