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Mostrando 181 - 200 Resultados de 20,270 Para Buscar 'Flavina~', tiempo de consulta: 2.87s Limitar resultados
  1. 181
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    Predicting Flavin and Nicotinamide Adenine Dinucleotide-Binding Sites in Proteins Using the Fragment Transformation Method
  2. 182
    “…Reductive cleavage of the disulfide in the presence of flavin mononucleotide (FMN) resulted in the reversible formation of a stable flavocytochrome. …”
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    Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.
  3. 183
    “…This process is facilitated by soluble, biogenic flavins secreted by the organism for the purpose of acting as an electron shuttle. …”
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    Flavin Binding to the Deca-heme Cytochrome MtrC: Insights from Computational Molecular Simulation
  4. 184
    “…The results evidence how the protein environment inversely functionalizes two flavins to switch from low-potential one-electron to hydride transfer at the thermodynamic limit of flavin redox chemistry.…”
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    Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
  5. 185
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    Structural Insights into Catalytic Versatility of the Flavin-dependent Hydroxylase (HpaB) from Escherichia coli
  6. 186
    “…The UbiX-UbiD enzymes are widespread in microbes, acting in concert to decarboxylate alpha-beta unsaturated carboxylic acids using a highly modified flavin cofactor, prenylated FMN (prFMN). UbiX serves as the flavin prenyltransferase, extending the isoalloxazine ring system with a fourth non-aromatic ring, derived from sequential linkage between a dimethylallyl moiety and the FMN N5 and C6. …”
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    The UbiX flavin prenyltransferase reaction mechanism resembles class I terpene cyclase chemistry
  7. 187
    “…Serum TMAO concentrations are significantly increased in CKD patients, which may be due in part to increased hepatic flavin monooxygenase (FMO)-mediated TMAO formation. …”
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    Metabolic Activation of Flavin Monooxygenase-mediated Trimethylamine-N-Oxide Formation in Experimental Kidney Disease
  8. 188
    “…Indigo is currently produced by a century-old petrochemical-based process, therefore it is highly attractive to develop a more environmentally benign and efficient biotechnological process to produce this timeless dye. Flavin-containing monooxygenases (FMOs) are able to oxidize a wide variety of substrates. …”
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    Structure-Based Redesign of a Self-Sufficient Flavin-Containing Monooxygenase towards Indigo Production
  9. 189
    “…Here, the first crystal structure of human MICAL3, which contains the flavin-containing monooxygenase (FMO) and calponin-homology (CH) domains, is reported. …”
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    Structural and kinetic insights into flavin-containing monooxygenase and calponin-homology domains in human MICAL3
  10. 190
    “…BACKGROUND: The aim of the present study was to investigate whether the disappearance of ischemic post-processing (IPO) in the myocardium of diabetes mellitus (DM) is associated with the increase of succinate dehydrogenase-flavin protein (SDHA). METHODS: A total of 50 Sprague Dawley rats, weighing 300–400 g, were divided into 5 groups according to the random number table method, each with 10 rats. …”
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    The disappearance of IPO in myocardium of diabetes mellitus rats is associated with the increase of succinate dehydrogenase-flavin protein
  11. 191
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    A dedicated flavin-dependent monooxygenase catalyzes the hydroxylation of demethoxyubiquinone into ubiquinone (coenzyme Q) in Arabidopsis
  12. 192
    “…The ubiquitous UbiD family of reversible decarboxylases is implicated in a wide range of microbial processes and depends on the prenylated flavin mononucleotide cofactor for catalysis. However, only a handful of UbiD family members have been characterized in detail, and comparison between these has suggested considerable variability in enzyme dynamics and mechanism linked to substrate specificity. …”
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    Structural and biochemical characterization of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decarboxylase
  13. 193
    “…Flavin mononucleotide (biobased flavin), widely known as FMN, possesses intrinsic fluorescence characteristics. …”
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    Color-changing intensified light-emitting multifunctional textiles via digital printing of biobased flavin
  14. 194
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    Flavin adenine dinucleotide-capped gold nanoclusters: biocompatible photo-emissive nanomaterial and reservoir of lumichrome
  15. 195
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    Site-Differentiated Iron–Sulfur Cluster Ligation Affects Flavin-Based Electron Bifurcation Activity
  16. 196
    “…Subsequent molecular docking and molecular dynamics simulations (MDs) for a cumulative duration of 2.1 microseconds revealed that ZINC003977803 (Diosmin) and ZINC008215434 (Flavin adenine dinucleotide-FAD) could be potential inhibitors against the E8 protein with the MM/GBSA binding free energies of −38.19 ± 9.69 and −35.59 ± 7.65 kcal·mol(−1), respectively.…”
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    Identification of Diosmin and Flavin Adenine Dinucleotide as Repurposing Treatments for Monkeypox Virus: A Computational Study
  17. 197
    “…In this work, we made use of the vast amount of sequence information that is currently available on protein databases to investigate the naturally occurring diversity of L-lactate-utilizing enzymes of the flavin mononucleotide (FMN)-dependent α-hydroxy acid oxidoreductase (HAOx) family. …”
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    Flavin Mononucleotide-Dependent l-Lactate Dehydrogenases: Expanding the Toolbox of Enzymes for l-Lactate Biosensors
  18. 198
    “…[Image: see text] Blue light sensing using flavin (BLUF) domains constitute a family of flavin-binding photoreceptors of bacteria and eukaryotic algae. …”
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    Spectroscopic and Computational Observation of Glutamine Tautomerization in the Blue Light Sensing Using Flavin Domain Photoreaction
  19. 199
    “…The flavin monooxygenase (FMO) enzyme was discovered in mammalian liver cells that convert a carcinogenic compound, N-N′-dimethylaniline, into a non-carcinogenic compound, N-oxide. …”
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    Genomic Survey of Flavin Monooxygenases in Wild and Cultivated Rice Provides Insight into Evolution and Functional Diversities
  20. 200
    “…Cellular redox ratios can be retrieved from fluorescence emitted by the coenzymes reduced nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD). Recent studies point out that the influence of flavin mononucleotide (FMN) has been underestimated. …”
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    Flavin fluorescence lifetime and autofluorescence optical redox ratio for improved visualization and classification of brain tumors
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