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Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins.
Deazaflavins have been found to act as potent catalysts in the photoreduction of flavoproteins in the presence of EDTA and other "photosubstrates". In distinction to the catalysis brought about byExpand
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Light-absorption studies on neutral flavin radicals.
Quantitative light absorption data of the neutral free flavosemiquinone are reported. It is shown that the visible range of the spectrum of the radical is drastically dependent on the solvent. TheExpand
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Basicity, visible spectra, and electron spin resonance of flavosemiquinone anions.
The dependence on pH of the disproportionation of the flavosemiquinone has been investigated by ESR. For 3-alkylated lumiflavin [R(3)=CH2COO−] in aqueous solution pK (for the dissociation of theExpand
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Light-induced alkylation and dealkylation of the flavin nucleus. Stable dihydroflavins: spectral course and mechanism of formation.
The spectral course of irreversible photoreduction of the flavin nucleus by arylacetates and related compounds has been investigated in detail. The resulting benzylated dihydroflavins and theirExpand
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Chemistry and molecular biology of flavins and flavoproteins
Despite the ubiquity of flavoproteins in nature, the working mechanisms of flavins are not well understood at a “molecular” level. In fact, flavocoenzymes are largely neglected as chemical entities,Expand
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Light-mediated reduction of flavoproteins with flavins as catalysts.
It has been found that small amounts of free flavins greatly accelerate the photochemical reduction of flavoproteins both to the radical and fully reduced oxidation states. This catalytic effect hasExpand
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Distinction of 2e- and 1e- reduction modes of the flavin chromophore as studied by flash photolysis.
Evidence is given for the fact that the excited flavin triplet (3Flox) exhibits competitive 1e- and 2e- transfer chemistry, depending on the nature of the photosubstrate. As an 'external'Expand
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Human ribosomal protein L7 carries two nucleic acid-binding domains with distinct specificities.
Protein L7 is associated with the large subunit of eukaryotic ribosomes that can act as a co-regulator of nuclear receptor-mediated transcription. In this study we show that L7 carries in addition toExpand
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Structure of a novel flavin chromophore from Avena coleoptiles, the possible 'blue light' photoreceptor.
A yellow chromophore has been isolated from Avena coleoptiles grown in the dark. It had previously been shown by Zenk [Zenk, M. H. (1967) Z. Pflanzenphysiol. 56, 122 - 140] to be a flavin of stillExpand
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