Effect of toxic ligands on O2 binding to heme and their toxicity mechanism-Reference-Cited by-同舟云学术

Effect of toxic ligands on O2 binding to heme and their toxicity mechanism

Published:2019 Issue:27 Volume:21 Page:14957-14963
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Li Renyi¹²³⁴^ORCID,Dai Xianqi¹²³⁴,Feng Zhen¹²³⁴,Li Yi¹²³⁴,Zhao Mingyu¹²³⁴,Liu Jing¹²³⁴^ORCID,Li Huiting¹²³⁴,Chen Yang¹²³⁴,Ma Yaqiang¹²³⁴,Tang Yanan⁵⁶⁷⁸⁴^ORCID

Affiliation:

1. College of Physics and Materials Science

2. Henan Normal University

3. Xinxiang

4. China

5. Quantum Materials Research Center

6. College of Physics and Electronic Engineering

7. Zhengzhou Normal University

8. Zhengzhou 450044

Abstract

Heme, as the cofactor and active site of Hb, enables Hb to carry out the necessary function required for O₂ management for life, that is, reversible O₂ binding for transport.

Funder

National Natural Science Foundation of China

Natural Science Foundation of Henan Province

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP02583A

Reference47 articles.

1. Mechanisms of Ligand Recognition in Myoglobin

2. Theoretical research on the charge transport properties of imidazoles axial-coordinated with protoheme molecule

3. A ferrous, high-spin heme a model for cytochrome a3 in the dioxygen reducing site of cytochrome oxidase

4. Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins

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