An intramolecular disulfide bond designed in myoglobin fine-tunes both protein structure and peroxidase activity-Reference-Cited by-同舟云学术

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An intramolecular disulfide bond designed in myoglobin fine-tunes both protein structure and peroxidase activity

Published:2016-06 Issue: Volume:600 Page:47-55
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Wu Lei-Bin,Yuan Hong,Zhou Hu,Gao Shu-Qin,Nie Chang-Ming,Tan Xiangshi,Wen Ge-Bo,Lin Ying-Wu

Funder

National Science Foundation of China

Hunan Provincial Natural Science Foundation

University of South China

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference52 articles.

1. Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

2. Design of functional metalloproteins

3. A designed supramolecular protein assembly with in vivo enzymatic activity

4. Artificial metalloenzymes derived from three-helix bundles

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1. Depth filtration of dredged sediments via reduced iron driving persulfate sodium activation: Perspectives from technical viability, potential mechanism, and prospect assessment;Journal of Cleaner Production;2024-09

2. Functional metalloenzymes based on myoglobin and neuroglobin that exploit covalent interactions;Journal of Inorganic Biochemistry;2024-08

3. Peroxidase activity of rice (Oryza sativa) hemoglobin: distinct role of tyrosines 112 and 151;JBIC Journal of Biological Inorganic Chemistry;2023-07-29

4. Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere;Chemical Reviews;2022-07-11

5. The X‐ray crystal structure of human A15C neuroglobin reveals both native/de novo disulfide bonds and unexpected ligand‐binding sites;Proteins: Structure, Function, and Bioinformatics;2022-01-10

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