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8.8
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Antioxidants
Special Issues
Methionine Oxidation and Reduction
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Methionine Oxidation and Reduction

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Aberrant Oxidation of Biomolecules".

Deadline for manuscript submissions: closed (20 August 2023) | Viewed by 4336

Special Issue Editor

Dr. Byung Cheon Lee

E-Mail Website
Guest Editor
College of Life Sciences and Biotechnology, Korea University, Seoul 02841, Republic of Korea
Interests: methionine oxidation; methionine restriction; aging; methionine sulfoxide reductase; redox biosensors
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Methionine is an essential amino acid that is necessary for various metabolisms, including the production of cysteine, glutathione, and S-adenosylmethionine, as well as protein synthesis. However, methionine is readily oxidized to methionine sulfoxide by reactive oxygen species (ROS) due to its sulfur-containing nature, which is often associated with malfunction in proteins and pathophysiological conditions under oxidative stress. Methionine sulfoxide is composed of two diastereomers, methionine-S-sulfoxide and methionine-R-sulfoxide, all of which are reduced by MsrA and MsrB, respectively. Accordingly, redox status change of methionine under various conditions has been studied to understand how methionine oxidation is implicated in the incidence of various disorders and the progress of aging or how the reduction of methionine sulfoxides is adopted to regulate protein function.

We invite you to submit your latest research findings or a review article to this Special Issue, which will bring together current research concerning methionine oxidation and reduction. We welcome submissions concerning all manipulation of methionine oxidation in diseases and aging, reversible methionine oxidation/reduction in regulating protein function and metabolism, methionine supplementation in redox signaling, and other methionine oxidation/reduction-related topics.

We look forward to your contributions.

Dr. Byung Cheon Lee
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antioxidants is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • methionine oxidation
  • methionine sulfoxide
  • oxidative stress
  • reactive oxygen species
  • aging
  • methionine sulfoxide reductase
  • redox signaling
  • regulation of protein function

Published Papers (2 papers)

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Research

18 pages, 1891 KiB  
Article
The Peptide Methionine Sulfoxide Reductase (MsrAB) of Haemophilus influenzae Repairs Oxidatively Damaged Outer Membrane and Periplasmic Proteins Involved in Nutrient Acquisition and Virulence
by Marufa Nasreen, Remya Purushothaman Nair, Alastair G. McEwan and Ulrike Kappler
Antioxidants 2022, 11(8), 1557; https://0-doi-org.brum.beds.ac.uk/10.3390/antiox11081557 - 11 Aug 2022
Cited by 3 | Viewed by 1978
Abstract
Sulfoxide-damage repair mechanisms are emerging as essential for the virulence of bacterial pathogens, and in the human respiratory pathogen Haemophilus influenzae the periplasmic MsrAB peptide methionine sulfoxide reductase is necessary for resistance to reactive chlorine species such as hypochlorite. Additionally, this enzyme has [...] Read more.
Sulfoxide-damage repair mechanisms are emerging as essential for the virulence of bacterial pathogens, and in the human respiratory pathogen Haemophilus influenzae the periplasmic MsrAB peptide methionine sulfoxide reductase is necessary for resistance to reactive chlorine species such as hypochlorite. Additionally, this enzyme has a role in modulating the host immune response to infection. Here, we have analysed the enzymatic properties of MsrAB, which revealed that both domains of the protein are catalytically active, with the turnover number of the MsrA domain being 50% greater than that for the MsrB domain. MsrAB was active with small molecular sulfoxides as well as oxidised calmodulin, and maximal activity was observed at 30°C, a temperature close to that found in the natural niche of H. influenzae, the nasopharynx. Analyses of differential methionine oxidation identified 29 outer membrane and periplasmic proteins that are likely substrates for MsrAB. These included the LldD lactate dehydrogenase and the lipoprotein eP4 that is involved in NAD and hemin metabolism in H. influenzae. Subsequent experiments showed that H. influenzae MsrAB can repair oxidative damage to methionines in purified eP4 with up to 100% efficiency. Our work links MsrAB to the maintenance of different adhesins and essential metabolic processes in the H. influenzae, such as NAD metabolism and access to L-lactate, which is a key growth substrate for H. influenzae during infection. Full article
(This article belongs to the Special Issue Methionine Oxidation and Reduction)
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19 pages, 2596 KiB  
Article
A Census of Human Methionine-Rich Prion-like Domain-Containing Proteins
by Juan Carlos Aledo
Antioxidants 2022, 11(7), 1289; https://0-doi-org.brum.beds.ac.uk/10.3390/antiox11071289 - 29 Jun 2022
Viewed by 1756
Abstract
Methionine-rich prion-like proteins can regulate liquid–liquid phase separation processes in response to stresses. To date, however, very few proteins have been identified as methionine-rich prion-like. Herein, we have performed a computational survey of the human proteome to search for methionine-rich prion-like domains. We [...] Read more.
Methionine-rich prion-like proteins can regulate liquid–liquid phase separation processes in response to stresses. To date, however, very few proteins have been identified as methionine-rich prion-like. Herein, we have performed a computational survey of the human proteome to search for methionine-rich prion-like domains. We present a census of 51 manually curated methionine-rich prion-like proteins. Our results show that these proteins tend to be modular in nature, with molecular sizes significantly greater than those we would expect due to random sampling effects. These proteins also exhibit a remarkably high degree of spatial compaction when compared to average human proteins, even when protein size is accounted for. Computational evidence suggests that such a high degree of compactness might be due to the aggregation of methionine residues, pointing to a potential redox regulation of compactness. Gene ontology and network analyses, performed to shed light on the biological processes in which these proteins might participate, indicate that methionine-rich and non-methionine-rich prion-like proteins share gene ontology terms related to the regulation of transcription and translation but, more interestingly, these analyses also reveal that proteins from the methionine-rich group tend to share more gene ontology terms among them than they do with their non-methionine-rich prion-like counterparts. Full article
(This article belongs to the Special Issue Methionine Oxidation and Reduction)
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