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Antioxidants
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The Janus Face of Oxidative Stress in Normal and Pathological...
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The Janus Face of Oxidative Stress in Normal and Pathological Conditions

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Health Outcomes of Antioxidants and Oxidative Stress".

Deadline for manuscript submissions: 31 January 2025 | Viewed by 1146

Special Issue Editor

Dr. Marco Fiore

E-Mail Website
Guest Editor
Institute of Biochemistry and Cell Biology (IBBC), National Research Council (CNR), Department of Sense Organs, University Sapienza of Rome, Viale del Policlinico, Rome, Italy
Interests: neurobiology; endocrinology; neurotrophins; oxidative stress; cancer; toxicology; addiction; antioxidants; polyphenols; alcohol use disorders
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue entitled "The Janus Face of Oxidative Stress in Normal and Pathological Conditions" purposes to delve into the dualistic environment of oxidative stress, a phenomenon that plays a crucial role in both the conservation of cellular homeostasis and the evolution of various diseases. This collection of articles will discover the subtle balance between the beneficial and detrimental outcomes of reactive oxygen/nitrogen species (ROS/RNS), highlighting how these molecules, while indispensable for standard physiological functions such as signaling and immune response, can also drive pathological activities when their regulation is altered. By combining cutting-edge research and comprehensive reviews, this issue pursues to provide a greater understanding of the mechanisms underlying oxidative stress and disclose potential therapeutic approaches for moderating its harmful impacts in disorders such as cancer, addiction, immune-endocrine conditions, neurodegenerative diseases, and cardiovascular disorders. Through this double perspective, this Special Issue emphasizes the importance of context in oxidative stress research, highlighting that the same molecular events can lead to vastly different consequences depending on the cellular and systemic setting.

We welcome original research (clinical and preclinical data) and review articles relating to this hot topic.

Dr. Marco Fiore
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

  • ethanol
  • toxicity
  • abuse
  • addiction
  • binge drinking
  • oxidative stress
  • psychoactive drug
  • cancer
  • recreational drug
  • FASD

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Published Papers (1 paper)

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Research

18 pages, 2401 KiB  
Article
Mutations Selectively Evolving Peroxidase Activity Among Alternative Catalytic Functions of Human Glutathione Transferase P1-1
by Aram Ismail and Bengt Mannervik
Antioxidants 2024, 13(11), 1347; https://doi.org/10.3390/antiox13111347 - 2 Nov 2024
Viewed by 679
Abstract
Glutathione transferases are detoxication enzymes with broad catalytic diversity, and small alterations to the protein’s primary structure can have considerable effects on the enzyme’s substrate selectivity profile. We demonstrate that two point mutations in glutathione transferase P1-1 suffice to generate 20-fold enhanced non-selenium-dependent [...] Read more.
Glutathione transferases are detoxication enzymes with broad catalytic diversity, and small alterations to the protein’s primary structure can have considerable effects on the enzyme’s substrate selectivity profile. We demonstrate that two point mutations in glutathione transferase P1-1 suffice to generate 20-fold enhanced non-selenium-dependent peroxidase activity indicating a facile evolutionary trajectory. Designed mutant libraries of the enzyme were screened for catalytic activities with alternative substrates representing four divergent chemistries. The chemical reactions comprised aromatic substitution, Michael addition, thiocarbamoylation, and hydroperoxide reduction. Two mutants, R1 (Y109H) and an R1-based mutant V2 (Q40M-E41Q-A46S-Y109H-V200L), were discovered with 16.3- and 30-foldincreased peroxidase activity with cumene hydroperoxide (CuOOH) compared to the wildtype enzyme, respectively. The basis of the improved peroxidase activity of the mutant V2 was elucidated by constructing double-point mutants. The mutants V501 (Q40M-Y109H) and V503 (E41Q-Y109H) were found to have 20- and 21-fold improvements in peroxidase activity relative to the wildtype enzyme, respectively. The steady-state kinetic profiles of mutants R1 and V2 in the reduction of CuOOH were compared to the wildtype parameters. The kcat values for R1 and V2 were 34- and 57-fold higher, respectively, than that of the wildtype enzyme, whereas the mutant Km values were increased approximately 3-fold. A 10-fold increased catalytic efficiency (kcat/Km) in CuOOH reduction is accomplished by the Tyr109His point mutation in R1. The 23-fold increase of the efficiency obtained in V2 was caused by adding further mutations primarily enhancing kcat. In all mutants with elevated peroxidase activity, His109 played a pivotal role. Full article
(This article belongs to the Special Issue The Janus Face of Oxidative Stress in Normal and Pathological Conditions)
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