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Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case
Journal article   Open access   Peer reviewed

Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case

Reinhard Schweitzer-Stenner
Molecules (Basel, Switzerland), v 27(24), p8751
09 Dec 2022
PMID: 36557884
url
https://doi.org/10.3390/molecules27248751View
Published, Version of Record (VoR)CC BY V4.0 Open

Abstract

Cytochromes c - metabolism Electron Transport Heme - chemistry Models, Molecular Oxidation-Reduction
Heme proteins are known to perform a plethora of biologically important functions. This article reviews work that has been conducted on various class I cytochrome c proteins over a period of nearly 50 years. The article focuses on the relevance of symmetry-lowering heme-protein interactions that affect the function of the electron transfer protein cytochrome c. The article provides an overview of various, mostly spectroscopic studies that explored the electronic structure of the heme group in these proteins and how it is affected by symmetry-lowering deformations. In addition to discussing a large variety of spectroscopic studies, the article provides a theoretical framework that should enable a comprehensive understanding of the physical chemistry that underlies the function not only of cytochrome c but of all heme proteins.

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6 citations in Scopus

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Web of Science research areas
Biochemistry & Molecular Biology
Chemistry, Multidisciplinary
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