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Xanthine

About: Xanthine is a research topic. Over the lifetime, 4046 publications have been published within this topic receiving 129820 citations. The topic is also known as: Xanthine.


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Journal ArticleDOI
TL;DR: This conclusion supports a mechanism that does not involve such an interaction and which begins with base-assisted nucleophilic attack of the Mo(VI)-OH group on the C-8 of substrate, with concomitant hydride transfer to give Mo(IV)-SH; the EPR-active "very rapid" species then forms by one-electron oxidation and deprotonation to yield the E PR-detectable Mo(V)OS(OR) species.
Abstract: Xanthine oxidase is a molybdenum-containing enzyme that catalyzes the hydroxylation of xanthine and a wide variety of other aromatic heterocycles. In the course of the reaction with xanthine and substrates such as 2-hydroxy-6-methylpurine (HMP), the enzyme gives rise to a Mo(V) EPR signal, denoted "very rapid", that arises from an authentic catalytic intermediate. The two alternative catalytic mechanisms proposed for this enzyme differ critically in whether the distance between Mo and C8 of the purine nucleus in this intermediate is short enough to admit a direct bonding interaction. To examine this distance, we have performed 13C ENDOR measurements of the "very rapid" EPR signal generated by xanthine oxidase during reaction with 13C8-HMP. The resulting (13)C8 hyperfine tensor, A = [10.2(1), 7.0(1), 6.5(1)] MHz, is discussed in the framework of a detailed consideration of factors involved in extracting metrical parameters from an anisotropic hyperfine interaction composed of contributions from multiple sources, in particular, the effect of the local contributions from spin density on (13)C8. The analysis presented here gives a Mo...C distance whose value is expected to be ca. 2.7-2.9 A in the "very rapid" intermediates formed with both xanthine and HMP, consistent with plausible bond lengths for a Mo-O-C8 fragment where C8 is a trigonal-planar aromatic carbon. The difference from earlier conclusions is explained. The data thus do not support the existence of a direct Mo-C bond in the signal-giving species. This conclusion supports a mechanism that does not involve such an interaction and which begins with base-assisted nucleophilic attack of the Mo(VI)-OH group on the C-8 of substrate, with concomitant hydride transfer to the Mo=S group to give Mo(IV)-SH; the EPR-active "very rapid" species then forms by one-electron oxidation and deprotonation to yield the EPR-detectable Mo(V)OS(OR) species. We further discuss the complexities and limitations of the semiempirical method used to arrive at these conclusions.

55 citations

Journal ArticleDOI
TL;DR: Pentoxifylline ameliorates histopathologic signs of injury and decreases lipid peroxidation (TBARS) and normal xanthine oxidase-xanthine dehydrogenase ratios in the treated compared with IR-only animals imply that the protective effect of PTX is at least partially mediated through inhibition of xanthin oxidase.
Abstract: Background Intestinal ischemia-reperfusion (IR) injury results in cell destruction, which may be mediated by the generation of reactive oxygen species, potentially toxic metabolites of xanthine oxidase. Pentoxifylline (PTX) possesses a variety of biochemical and antioxidant properties that can improve capillary flow and tissue oxygenation. Because of these combined effects, it has been hypothesized that pentoxifylline would protect against intestinal IR. Methods Young adult rats were randomly assigned to one of four experimental groups: IR/Placebo (n = 12) in which superior and inferior mesenteric arteries were clamped for 45 minutes and then reopened; IR/PTX (n = 11) in which IR was induced as in the Placebo group, but with 25 mg/kg PTX at 0, 30, and 60 minutes; No IR/Placebo (n = 12); and No IR/PTX (n = 6) in which placebo and PTX were applied with no IR. Blood and intestinal samples were taken for serial thiobarbituric acid-reducing substances (TBARS; index of lipid peroxidation), for xanthine oxidase-xanthine dehydrogenase ratios, glutathione, myeloperoxidase, and histopathology. Results Animals in the IR/PTX group had lower TBARS and the least severe histopathologic injury. Xanthine oxidasexanthine dehydrogenase ratios were elevated only in IR/ Placebo (0.67+/-0.22 vs. 0.45+/-0.14 in IR/PTX; 0.42+/-0.22 in No IR/Placebo; and 0.40+/-0.11 in No IR/PTX; p = 0.0009). Reduced glutathione was diminished in IR/PTX animals (38.9 +/-1.35 vs. 46.1+/-7.0 in IR/Placebo; 41.1+/-2.5 in No IR/ Placebo; 43.6+/-1.0 in No IR/PTX; p = 0.048). No differences were recorded in myeloperoxidase levels among groups. Conclusions Pentoxifylline ameliorates histopathologic signs of injury and decreases lipid peroxidation (TBARS). Normal xanthine oxidase-xanthine dehydrogenase ratios in the treated compared with IR-only animals imply that the protective effect of PTX is at least partially mediated through inhibition of xanthine oxidase.

55 citations

Journal ArticleDOI
TL;DR: Results suggest that morphine increases striatal DA release and 5-hydroxytryptamine oxidative metabolism by a micro-opioid receptor-mediated mechanism mainly at extranigrostriatal sites and affects glutamate and AA release by amicro-opIOid receptor mediated mechanism acting also at nigral sites.

55 citations

Journal ArticleDOI
TL;DR: In this paper, a novel and sensitive amperometric xanthine biosensor was developed by preparing a nanocomposite film that was constructed by embedding reduced expanded graphene oxide (REGO) sheets decorated with iron oxide (Fe 3 O 4 ) nanoparticles into poly(glycidyl methacrylate-co-vinylferrocene) (P(GMA- co -VFc)) phase, and by covalent immobilization of Xanthine oxidase (XOD) on the surface of P(Gma-co)-

55 citations

Journal ArticleDOI
TL;DR: It is proposed that an important function of xanthine oxidase is to provide an ubiquitous source of hydrogen peroxide and superoxide radicals which serve as oxidants for coupled biological oxidations.
Abstract: The biochemical properties of tetrazolium reductase inhibitor (“reductase inhibitor”) from beef brain and liver were compared with superoxide dismutase (erythrocuprein) from beef erythrocytes, using xanthine oxidase and xanthine as a model system. In all assays the behavior of erythrocuprein and the reductase inhibitor was identical; it is concluded that the tetrazolium reductase inhibitor is a member of the superoxide dismutase class of enzymes. Its possible identity with other proteins of this group remains to be established. Xanthine dehydrogenase is activated by natural or synthetic detergents. These compounds eliminate the enzymatic action of both erythrocuprein and reductase inhibitor. Low levels of cyanide, which do not inhibit xanthine dehydrogenase block superoxide dismutase. The biological role of xanthine oxidase is discussed. We propose that an important function of xanthine oxidase is to provide an ubiquitous source of hydrogen peroxide and superoxide radicals which serve as oxidants for coupled biological oxidations.

54 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202361
2022108
202157
202060
201961
201869