Issue 13, 2022

On the roles of methionine and the importance of its microenvironments in redox metalloproteins

Abstract

The amino acid residue methionine (Met) is commonly thought of as a ligand in redox metalloproteins, for example in cytochromes c and in blue copper proteins. However, the roles of Met can go beyond a simple ligand. The thioether functional group of Met allows it to be considered as a hydrophobic residue as well as one that is capable of weak dipolar interactions. In addition, the lone pairs on sulphur allow Met to interact with other groups, inluding the aforementioned metal ions. Because of its properties, Met can play diverse roles in metal coordination, fine tuning of redox reactions, or supporting protein structures. These roles are strongly influenced by the nature of the surrounding medium. Herein, we describe several common interactions between Met and surrounding aromatic amino acids and how they affect the physical properties of both copper and iron metalloproteins. While the importance of interactions between Met and other groups is established in biological systems, less is known about their roles in redox metalloproteins and our view is that this is an area that is ready for greater attention.

Graphical abstract: On the roles of methionine and the importance of its microenvironments in redox metalloproteins

Article information

Article type
Perspective
Submitted
31 Dec 2021
Accepted
24 Feb 2022
First published
07 Mar 2022

Dalton Trans., 2022,51, 4976-4985

On the roles of methionine and the importance of its microenvironments in redox metalloproteins

C. A. Gibbs, B. P. Fedoretz-Maxwell and J. J. Warren, Dalton Trans., 2022, 51, 4976 DOI: 10.1039/D1DT04387K

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements