نتایج جستجو برای: مسیر 4s
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Single electron transfers have been examined in complex II (succinate:ubiquinone oxidoreductase) by the method of pulse radiolysis. Electrons are introduced into the enzyme initially at the [3Fe-4S] and ubiquinone sites followed by intramolecular equilibration with the b heme of the enzyme. To define thermodynamic and other controlling parameters for the pathways of electron transfer in complex...
Structural transformation of ezetimibe was performed by fungi Beauvaria bassiana and Cunninghamella blakesleeana. The metabolites were identified by different spectroscopic techniques as (3R,4S)-1-(4-fluorophenyl)-3-((E)-3-(4-fluorophenyl) allyl)-4-(4-hydroxyphenyl) azetidin-2-one (2), (3R, 4S)-1-(4-fluorophenyl)-3-(3-(4fluorophenyl)-3-oxopropyl)-4-(4-hydroxyphenyl) azetidin-2-one (3), (3R,4S) ...
The production of prompt J/ψ, ψ(2S), χc1 and χc2 is studied using a 32.4 fb data sample collected with the Belle detector at the Υ(4S) and 60 MeV below the resonance. The yield of prompt J/ψ mesons in the Υ(4S) sample is compatible with that of continuum production; we set an upper limit B(Υ(4S) → J/ψX) < 1.9 × 10−4 at the 95% confidence level, and find σ(e+e− → J/ψX) = 1.47 ± 0.10 ± 0.13 pb. T...
Context. The stellar abundance ratio of Mg/Fe is an important tool in diagnostics of galaxy evolution. In order to make reliable measurements of the Mg abundance of stars, it is necessary to have accurate values for the oscillator strength ( f -value) of each of the observable transitions. In metal-poor stars the Mg i 3p–4s triplet around 5175 Å (Fraunhofer’s so-called b lines) are the most pro...
The major DNA photoproduct of dormant, UV-irradiated Bacillus subtilis spores is the thymine dimer 5-thyminyl-5,6-dihydrothymine [spore photoproduct (SP)]. During spore germination, SP is reversed to two intact thymines in situ by the DNA repair enzyme SP lyase, an S-adenosylmethionine (S-AdoMet)-dependent iron-sulfur ([Fe-S]) protein encoded by the splB gene. In the present work, cross-linking...
Heterodisulfide reductase (HDR) of methanogenic archaea with its active-site [4Fe-4S] cluster catalyzes the reversible reduction of the heterodisulfide (CoM-S-S-CoB) of the methanogenic coenzyme M (CoM-SH) and coenzyme B (CoB-SH). CoM-HDR, a mechanistic-based paramagnetic intermediate generated upon half-reaction of the oxidized enzyme with CoM-SH, is a novel type of [4Fe-4S]3+ cluster with CoM...
DNA charge transport (CT) chemistry provides a route to carry out oxidative DNA damage from a distance in a reaction that is sensitive to DNA mismatches and lesions. Here, DNA-mediated CT also leads to oxidation of a DNA-bound base excision repair enzyme, MutY. DNA-bound Ru(III), generated through a flash/quench technique, is found to promote oxidation of the [4Fe-4S](2+) cluster of MutY to [4F...
Hybrid Chemo-, Bio-, and Electrocatalysis for Atom-Efficient Deuteration of Cofactors in Heavy Water
Deuterium-labeled nicotinamide cofactors such as [4-2H]-NADH can be used mechanistic probes in biological redox processes and offer a route to the synthesis of selectively [2H] labeled chemicals via biocatalytic reductive deuteration. Atom-efficient routes formation recycling are therefore highly desirable but require careful design order alleviate requirement for [2H]-labeled reducing agents. ...
In this paper, we are concerned with the following fractional Schrödinger-Poisson system: (−∆s)u + u + λφu = µf(u) +|u|p−2|u|, x ∈R3 (−∆t)φ = u2, x ∈R3 where λ,µ are two parameters, s,t ∈ (0,1] ,2t + 4s > 3 ,1 < p ≤ 2∗ s and f : R → R is continuous function. Using some critical point theorems and truncation technique, we obtain the existence and multiplicity of non-trivial solutions with ...
Pyruvate formate lyase activating enzyme is a member of a novel superfamily of enzymes that utilize S-adenosylmethionine to initiate radical catalysis. This enzyme has been isolated with several different iron-sulfur clusters, but single turnover monitored by EPR has identified the [4Fe-4S](1+) cluster as the catalytically active cluster; this cluster is believed to be oxidized to the [4Fe-4S](...
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