Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.17.3.2 (xanthine oxidase)
 8,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The synthesis of a heterodinucleating ligand LH2 (LH2 = (E)-3-(((2,7-di-tert-butyl-9,9-dimethyl-5-((pyridin-2-ylmethylene)amino)-9H-xanthen-4-yl)amino)methyl)benzene-1,2-diol) was undertaken toward a functional model of the bimetallic active site found in Mo-Cu carbon monoxide dehydrogenase (Mo-Cu CODH), and to understand the origins of heterobimetallic cooperativity exhibited by the enzyme. LH2 features a hard potentially dianionic catechol chelate for binding Mo(vi) and a soft iminopyridine chelate for binding Cu(i). Treatment of LH2 with either Cu(i) or M(vi) (M = Mo, W) sources leads to the anticipated site-selective incorporation of the respective metals. While both [CuI(LH2)]+ and [MVIO3(L)]2- complexes are stable in the solid state, [MVIO3(L)]2- complexes disproportionate in solution to give [MVIO2(L)2](NEt4)2 complexes, with [MVIO4]2- as the by-product. The incorporation of BOTH Mo(vi) and Cu(i) into L forms a highly reactive heterobimetallic complex [MoVIO3CuI(L)](NEt4)2, whose formation and reactivity was interrogated via1H NMR/UV-vis spectroscopy and DFT calculations. These studies reveal that the combination of the two metals triggers oxidation reactivity, in which a nucleophilic Mo(vi) trioxo attacks Cu(i)-bound imine. The major product of the reaction is a crystallographically characterized molybdenum(vi) complex [Mo(L')O2](NEt4) coordinated by a modified ligand L' that contains a new C-O bond in place of the imine functionality. This observed hydroxylation reactivity is consistent with the postulated first step of Mo-Cu CODH (nucleophilic attack of the Mo(vi)-oxo on the Cu(i)-bound electrophilic CO) and xanthine oxidoreductase (nucleophilic attack of Mo(vi)-oxo on the electrophilic xanthine carbon).
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PMID:Cooperative bimetallic reactivity of a heterodinuclear molybdenum-copper model of Mo-Cu CODH. 2994 11

Satureja montana herbal species belongs to aromatic medicinal plants with a significant place in traditional medicine. However, products produced with conventional procedures do not meet the requirements of the modern market which include environmentally-safe processes that provide quality, safe, and standardized products. In this study, the antiproliferative activity of S. montana extracts obtained by supercritical carbon dioxide and solid-liquid extraction followed by spray drying was investigated using the in vivo model of Ehrlich ascites carcinoma (EAC) in mice. The impact of two concentrations of extracts on the growth of tumor and the redox status of malignant cells was monitored. It was determined that the extracts induced oxidative stress in the malignant cells which was confirmed by the changes in activity of biochemical indicators of oxidative stress. The posttreatment was not an efficient approach, while the extracts applied as pretreatment and treatment resulted in an increase in the xanthine oxidase (XOD) activity, a decrease in catalase (CAT) activity, and an increase in the intensity of lipid peroxidation (LPx). Furthermore, a decrease in the values of reduced glutathione (GSH) and an increase in glutathione reductase (GR) and glutathione peroxidase (GSHPx) in EAC cells were recorded.
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PMID:Evaluation of Anticancer Activity of Satureja montana Supercritical and Spray-Dried Extracts on Ehrlich's Ascites Carcinoma Bearing Mice. 3318 63


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