Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme Proteins-Reference-Cited by-同舟云学术

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Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme Proteins

Published:2022-12-09 Issue:51 Volume:61 Page:20949-20963
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Zhong Fangfang¹^ORCID,Albert Therese²^ORCID,Moënne-Loccoz Pierre²^ORCID,Pletneva Ekaterina V.¹^ORCID

Affiliation:

1. Department of Chemistry, Dartmouth College, Hanover, New Hampshire 03755, United States

2. Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, Oregon 97239, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.inorgchem.2c03427

Reference80 articles.

1. Heme: emergent roles of heme in signal transduction, functional regulation and as catalytic centres

2. How Cytochromes with Different Folds Control Heme Redox Potentials

3. Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere

4. Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

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1. The structure of the diheme cytochrome c4 from Neisseria gonorrhoeae reveals multiple contributors to tuning reduction potentials;Journal of Inorganic Biochemistry;2024-04

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