| InChI=1S/C6H4N4O2/c11-5-3-4(8-2-1-7-3)9-6(12)10-5/h1-2H,(H2,8,9,10,11,12) |
| UYEUUXMDVNYCAM-UHFFFAOYSA-N |
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1H,3H-pteridine-2,4-dione
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IUBMB
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2,4(3H,8H)-Pteridinedione
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KEGG COMPOUND
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2,4-Dihydroxypteridine
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KEGG COMPOUND
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2,4-dihydroxypteridine
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UniProt
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Lumazine
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KEGG COMPOUND
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Pteridine-2,4-dione
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KEGG COMPOUND
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487-21-8
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CAS Registry Number
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KEGG COMPOUND
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487-21-8
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CAS Registry Number
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ChemIDplus
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610331
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Reaxys Registry Number
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Reaxys
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Moyon NS, Islam MM, Phukan S, Mitra S (2013)
Fluorescence modulation and associative behavior of lumazine in hydrophobic domain of micelles and bovine serum albumin.
Journal of photochemistry and photobiology. B, Biology 121, 37-45 [PubMed:23501728]
[show Abstract]
The photophysical behavior of the deprotonated form of lumazine (Lum-anion) was studied in biologically relevant surfactant systems like sodium dodecyl sulfate (SDS), cetyltrimethylammonium bromide (CTAB) and TritonX-100 (TX-100) and also model water soluble protein, bovine serum albumin (BSA), using steady-state and time-resolved fluorescence spectroscopy in buffer solution of pH 12.0. The association constant values were calculated from modulated fluorescence intensity of Lum-anion in different medium. The interaction of non-ionic surfactant TX-100 was found to be about 10 times greater than SDS and CTAB. However, while the driving force of binding in SDS and/or TX-100 is mainly hydrophobic in nature, electrostatic interaction with the oppositely charged micellar head group is the predominant factor in CTAB. The thermodynamic parameters like enthalpy (ΔH) and entropy (ΔS) change, etc., corresponding to the binding of Lum-anion with BSA were estimated by performing the fluorescence titration experiment at different temperatures. Thermodynamically favorable and strong binding of Lum-anion (K~10(4) M(-1)) into BSA is due to hydrophobic interaction in the ligand binding domain II. However, the binding mechanism is entirely different in presence of protein denaturing agent like urea and electrostatic interaction plays a major role under this condition. | West AE, Schimdt SK (2002)
Endogenous methanogenesis stimulates oxidation of atmospheric CH(4) in alpine tundra soil.
Microbial ecology 43, 408-415 [PubMed:12043000]
[show Abstract]
Experiments were done to test the hypothesis that atmospheric CH(4) oxidizers in a well-drained alpine tundra soil are supported by CH(4) production from anaerobic microsites in the soil. Soil was subjected to 22 days of anaerobic conditions with elevated H(2) and CO(2) in order to stimulate methanogenesis. This treatment stimulated subsequent atmospheric CH(4) consumption, probably by increasing soil methanogenesis. After removal from anaerobic conditions, soils emitted CH(4) for up to 6 h, then oxidized atmospheric CH(4) at 111 (+/- 5.7) pmol (g dry weight)(-1) h(-1), which was more than 3 times the rate of control soils. Further supporting our hypothesis, additions of lumazine, a highly specific inhibitor of methanogenesis, prevented the stimulation of atmospheric CH(4) oxidation by the anaerobic treatment. The method used to create anaerobic conditions with elevated H(2) and CO(2) also elevated headspace CH(4) concentrations. However, elevated CH(4) concentrations under aerobic conditions did not stimulate CH(4) oxidation as much as preexposure to H(2) and CO(2) under anaerobic conditions. Anaerobic conditions created by N(2) flushing did not stimulate atmospheric CH4 oxidation, probably because N2 flushing inhibited methanogenesis by removing necessary precursors for methane production. We conclude that anaerobic conditions with elevated H(2) and CO(2) stimulate atmospheric CH(4) oxidation in this dry alpine tundra soil by increasing endogenous CH(4) production. This effect was prevented by inhibiting methanogenesis, indicating the importance of endogenous CH(4) production in a CH(4-) consuming soil. |
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