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      • Record: found
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      Protein thiyl radical reactions and product formation: a kinetic simulation

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          Abstract

          Protein thiyl radicals are important intermediates generated in redox processes of thiols and disulfides. Thiyl radicals efficiently react with glutathione and ascorbate, and the common notion is that these reactions serve to eliminate thiyl radicals before they can enter potentially hazardous processes. However, over the past years increasing evidence has been provided for rather efficient intramolecular hydrogen transfer processes of thiyl radicals in proteins and peptides. Based on rate constants published for these processes, we have performed kinetic simulations of protein thiyl radical reactivity. Our simulations suggest that protein thiyl radicals enter intramolecular hydrogen transfer reactions to a significant extent even under physiologic conditions, i.e. in the presence of 30 μM oxygen, 1 mM ascorbate and 10 mM glutathione. At lower concentrations of ascorbate and glutathione, frequently observed when tissue is exposed to oxidative stress, the extent of irreversible protein thiyl radical-dependent protein modification increases.

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          Oxidative stress in blood in Alzheimer's disease and mild cognitive impairment: a meta-analysis.

          M Zabel, O Ghribi, R. Squitti … (2013)
          Abnormal oxidative stress is an established feature of Alzheimer's disease, but clinical trials aiming to reduce oxidative stress have not yet proven an effective therapy for dementia patients. The purpose of this review is to systematically analyze available data describing markers of oxidative stress and antioxidants in blood from subjects with Alzheimer's disease or those with mild cognitive impairment to highlight potential interactions between peripheral redox changes and central nervous system pathology and contribute to the design of future clinical study. PubMed, SCOPUS and Web of Science were systematically queried to collect studies which have evaluated markers of oxidative stress, levels of antioxidants, copper, transferrin and ceruloplasmin levels in blood from subjects with Alzheimer's disease and matched controls. After application of quality measures, results were aggregated in a random effects analysis. We found that markers of lipid peroxidation are elevated in blood in Alzheimer's disease and in mild cognitive impairment, copper metabolism is dysregulated and total antioxidant capacity is decreased. While surprisingly none of the major antioxidative enzymes are significantly decreased, non-enzymatic antioxidants in blood (particularly uric acid, vitamins A, E and C, α- and β-carotene) are significantly decreased. There is significant oxidative damage in peripheral blood early in the process of neurodegeneration. We propose that clinical studies assessing cognitive outcomes after antioxidant therapy tailor interventions to individual patients' deficiencies and confirm an improvement in an appropriate serological marker of oxidative stress. This strategy may be most effectively applied in a clinical trial of primary prevention. © 2013.
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            Electrode potentials of partially reduced oxygen species, from dioxygen to water.

            Willem Koppenol, David M Stanbury, Patricia L. Bounds (2010)
            We use published Gibbs energies of formation and equilibrium constants to determine electrode potentials for the partially reduced intermediates along the pathway of reduction of dioxygen to water, as well as of ozone and singlet dioxygen. The results are summarized in an oxidation state (Frost) diagram. Our review of the literature on electrode potentials leads us to revise values for the O(2)/O(2)(*-) couple to E degrees (O(2g)/O(2)(*-))=-0.35+/-0.02V and E degrees (O(2aq)/O(2)(*-))=-0.18+/-0.02V from -0.33 and -0.16V, respectively. Other electrode potentials (pH 7) for the radical species covered are E degrees '(O(3g)/O(3)(*-))=+0.91V, E degrees '(HO(2)(*), H(+)/H(2)O(2))=+1.05V, E degrees '(H(2)O(2), H(+)/HO(*), H(2)O)=+0.39V, and E degrees '(HO(*), H(+)/H(2)O)=+2.31V. Copyright 2010 Elsevier Inc. All rights reserved.
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              Iron homeostasis, oxidative stress, and DNA damage.

              R Meneghini (1996)
              Cellular DNA damage under prooxidant conditions has been shown to be mediated by iron. In fact, iron is an important element in the establishment of a prooxidant status in the cell. It is discussed that there exists a mutual dependence between iron metabolism and oxidative stress. Changes in the former by means of genetic manipulation bring about modification in the redox status as judge by oxidative damage in DNA. On the other hand, the induction of a cellular prooxidative condition activates the protein IRP (iron regulatory protein) in a way that renders the cell more able to take up iron. The possible implications of these results is discussed in the light of recent findings reported in the literature on hydrogen peroxide as a signaling species for cell proliferation. The question of DNA strand break formation under prooxidant conditions is reviewed from the viewpoint of which agent is more important: an oxidant generated by Fenton type reaction or Ca2+-activated nucleases. The presence of iron in the nucleus is reviewed. Results have been produced indicating that the larger concentration of this metal in the nucleus, as compared to the cytosol, seems to be explained by an iron-type P-ATPase. There is no explanation, presently, for iron presence in the nucleus, but it certainly imposes a prooxidant trend that needs to be counterbalanced in some way, and evidence is reviewed that nuclear metallothionein plays a role in this regard.
              Article 0 comments Cited 53 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-journal-id): 8709159
                Journal ID (pubmed-jr-id): 3902
                Journal ID (nlm-ta): Free Radic Biol Med
                Journal ID (iso-abbrev): Free Radic. Biol. Med.
                Title: Free radical biology & medicine
                ISSN (Print): 0891-5849
                ISSN (Electronic): 1873-4596
                Publication date Nihms-submitted: 2 November 2016
                Publication date (Electronic): 12 December 2014
                Publication date (Print): March 2015
                Publication date PMC-release: 22 November 2016
                Volume: 80
                Pages: 158-163
                Affiliations
                [1 ]Institute of Inorganic Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, 8093 Zürich, Switzerland
                [2 ]Department of Pharmaceutical Chemistry, The University of Kansas, 2095 Constant Avenue, Lawrence, KS 66047, USA
                Author notes
                Correspondence: T. Nauser ( nauser@ 123456inorg.chem.ethz.ch ); Ch. Schöneich ( schoneic@ 123456ku.edu )
                Article
                Manuscript ID: NIHMS662058
                DOI: 10.1016/j.freeradbiomed.2014.12.006
                PMC ID: 5118936
                PubMed ID: 25499854
                SO-VID: 2d69387f-82fc-4370-8dab-e61ca9408b06
                License:

                This manuscript version is made available under the CC BY-NC-ND 4.0 license.

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                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: thiyl radicals,hydrogen atom transfer,carbon-centered radicals,d-amino acids,glutathione
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: thiyl radicals, hydrogen atom transfer, carbon-centered radicals, d-amino acids, glutathione

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