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Redox Stress in Bioinorganic Chemistry
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Redox Stress in Bioinorganic Chemistry

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Inorganic Chemistry".

Deadline for manuscript submissions: 31 May 2024 | Viewed by 2028

Special Issue Editor

Prof. Dr. Radu Silaghi-Dumitrescu

E-Mail Website
Guest Editor
The Faculty of Chemistry and Chemical Engineering, Babes-Bolyai University, Cluj-Napoca, Romania
Interests: bioinorganic chemistry; redox; oxidative stress; computational chemistry; coordination chemistry

Special Issue Information

Dear Colleagues,

Biological redox stress entails imbalances in the supply/demand of electrons and/or changes in concentrations of particularly reactive redox species with effects on biomedically relevant phenomena such as disease, aging, immunity, or microbial evolution/adaptation. Most often, this involves molecules with oxidative potential, within the framework of the well-known oxidative stress; this would include reactive oxygen species (generally, partially reduced, and/or excited versions of molecular oxygen), as well as organic free radicals generated therefrom. Nitrogen-based stress agents (primarily nitrogen oxides and oxyanions, accounting for the more recently defined nitrosative stress) or reactive sulfur species, as well as others (e.g., selenium, or halide oxides/oxyanions) can also cause forms of redox stress. An excess of reducing agents would define the opposite of oxidative stress—namely, reducing stress. Bioinorganic chemistry may offer insight into the nature of the inorganic redox stress agents, as well as on a wide range of biological metal centers that are involved in the generation, mitigation, or adaptation to redox stress. This Special Issue aims to give an overview of the most recent advances in the field of the bioinorganic aspects of biological redox stress.

Potential topics include but are not limited to:

  • Reactive oxygen species in biology;
  • Reactive nitrogen species in biology;
  • Reactive sulfur species in biology;
  • Reactive halogen species in biology;
  • New developments in the mechanism, function, and applications of antioxidant metalloenzymes;
  • Molecular mechanisms entailing biological metal centers and redox stress in disease;
  • New analytical tools and methodology for investigating the role and mechanisms of biological metal centers in redox stress.

Prof. Dr. Radu Silaghi-Dumitrescu
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. Molecules is an international peer-reviewed open access semimonthly 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 2700 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

  • metalloprotein
  • metalloenzyme
  • oxidative stress
  • nitrosative stress
  • redox stress

Published Papers (2 papers)

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Research

19 pages, 3774 KiB  
Article
Redox Reactivity of Nonsymbiotic Phytoglobins towards Nitrite
by Cezara Zagrean-Tuza, Galaba Pato, Grigore Damian, Radu Silaghi-Dumitrescu and Augustin C. Mot
Molecules 2024, 29(6), 1200; https://doi.org/10.3390/molecules29061200 - 07 Mar 2024
Viewed by 1093
Abstract
Nonsymbiotic phytoglobins (nsHbs) are a diverse superfamily of hemoproteins grouped into three different classes (1, 2, and 3) based on their sequences. Class 1 Hb are expressed under hypoxia, osmotic stress, and/or nitric oxide exposure, while class 2 Hb are induced by cold [...] Read more.
Nonsymbiotic phytoglobins (nsHbs) are a diverse superfamily of hemoproteins grouped into three different classes (1, 2, and 3) based on their sequences. Class 1 Hb are expressed under hypoxia, osmotic stress, and/or nitric oxide exposure, while class 2 Hb are induced by cold stress and cytokinins. Both are mainly six-coordinated. The deoxygenated forms of the class 1 and 2 nsHbs from A. thaliana (AtHb1 and AtHb2) are able to reduce nitrite to nitric oxide via a mechanism analogous to other known globins. NsHbs provide a viable pH-dependent pathway for NO generation during severe hypoxia via nitrite reductase-like activity with higher rate constants compared to mammalian globins. These high kinetic parameters, along with the relatively high concentrations of nitrite present during hypoxia, suggest that plant hemoglobins could indeed serve as anaerobic nitrite reductases in vivo. The third class of nsHb, also known as truncated hemoglobins, have a compact 2/2 structure and are pentacoordinated, and their exact physiological role remains mostly unknown. To date, no reports are available on the nitrite reductase activity of the truncated AtHb3. In the present work, three representative nsHbs of the plant model Arabidopsis thaliana are presented, and their nitrite reductase-like activity and involvement in nitrosative stress is discussed. The reaction kinetics and mechanism of nitrite reduction by nsHbs (deoxy and oxy form) at different pHs were studied by means of UV-Vis spectrophotometry, along with EPR spectroscopy. The reduction of nitrite requires an electron supply, and it is favored in acidic conditions. This reaction is critically affected by molecular oxygen, since oxyAtHb will catalyze nitric oxide deoxygenation. The process displays unique autocatalytic kinetics with metAtHb and nitrate as end-products for AtHb1 and AtHb2 but not for the truncated one, in contrast with mammalian globins. Full article
(This article belongs to the Special Issue Redox Stress in Bioinorganic Chemistry)
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16 pages, 3272 KiB  
Article
Influence of Equatorial Co-Ligands on the Reactivity of LFeIIIOIPh
by Dóra Lakk-Bogáth, Dénes Pintarics, Patrik Török and József Kaizer
Molecules 2024, 29(1), 58; https://doi.org/10.3390/molecules29010058 - 21 Dec 2023
Viewed by 634
Abstract
Previous biomimetic studies clearly proved that equatorial ligands significantly influence the redox potential and thus the stability/reactivity of biologically important oxoiron intermediates; however, no such studies were performed on FeIIIOIPh species. In this study, the influence of substituted pyridine co-ligands on [...] Read more.
Previous biomimetic studies clearly proved that equatorial ligands significantly influence the redox potential and thus the stability/reactivity of biologically important oxoiron intermediates; however, no such studies were performed on FeIIIOIPh species. In this study, the influence of substituted pyridine co-ligands on the reactivity of iron(III)-iodosylbenzene adduct has been investigated in sulfoxidation and epoxidation reactions. Selective oxidation of thioanisole, cis-cyclooctene, and cis- and trans-stilbene in the presence of a catalytic amount of [FeII(PBI)3](OTf)2 with PhI(OAc)2 provide products in good to excellent yields through an FeIIIOIPh intermediate depending on the co-ligand (4R-Py) used. Several mechanistic studies were performed to gain more insight into the mechanism of oxygen atom transfer (OAT) reactions to support the reactive intermediate and investigate the effect of the equatorial co-ligands. Based on competitive experiments, including a linear free-energy relationship between the relative reaction rates (logkrel) and the σp (4R-Py) parameters, strong evidence has been observed for the electrophilic character of the reactive species. The presence of the [(PBI)2(4R-Py)FeIIIOIPh]3+ intermediates and the effect of the co-ligands was also supported by UV-visible measurements, including the color change from red to green and the hypsochromic shifts in the presence of co-ligands. This is another indication that the title iron(III)-iodosylbenzene adduct is able to oxygenate sulfides and alkenes before it is transformed into the oxoiron form by cleavage of the O−I bond. Full article
(This article belongs to the Special Issue Redox Stress in Bioinorganic Chemistry)
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