Relevant bibliographies by topics / Flavin mono nucleotide (FMN)

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  1. Journal articles

Academic literature on the topic 'Flavin mono nucleotide (FMN)'

Author: Grafiati
Published: 7 June 2025
Last updated: 2 August 2025

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Journal articles on the topic "Flavin mono nucleotide (FMN)"

1

CUNNINGHAM, Orla, Michael G. GORE та Timothy J. MANTLE. "Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXβ reductase (BVR-B)". Biochemical Journal 345, № 2 (2000): 393–99. http://dx.doi.org/10.1042/bj3450393.

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The initial-rate kinetics of the flavin reductase reaction catalysed by biliverdin-IXβ reductase at pH 7.5 are consistent with a rapid-equilibrium ordered mechanism, with the pyridine nucleotide binding first. NADPH binding to the free enzyme was characterized using stopped-flow fluorescence quenching, and a Kd of 15.8 μM was calculated. Equilibrium fluorescence quenching experiments indicated a Kd of 0.55 μM, suggesting that an enzyme-NADPH encounter complex (Kd 15.8 μM) isomerizes to a more stable ‘nucleotide-induced’ conformation. The enzyme was shown to catalyse the reduction of FMN, FAD a
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2

Willetts, Andrew. "Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations." Microorganisms 11, no. 1 (2022): 71. http://dx.doi.org/10.3390/microorganisms11010071.

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Using highly purified enzyme preparations throughout, initial kinetic studies demonstrated that the isoenzymic 2,5- and 3,6-diketocamphane mono-oxygenases from Pseudomonas putida ATCC 17453 and the LuxAB luciferase from Vibrio fischeri ATCC 7744 exhibit commonality in being FMN-dependent two-component monooxygenases that promote redox coupling by the transfer of flavin reductase-generated FMNH2 by rapid free diffusion. Subsequent studies confirmed the comprehensive inter-species compatibility of both native and non-native flavin reductases with each of the tested monooxygenases. For all three
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3

Kashpur, V., O. Khorunzhaya, and D. Pesina. "Dielectrometry of hydration of fl avin mononucleotide and DNA." RADIOFIZIKA I ELEKTRONIKA 26, no. 3 (2021): 46–53. http://dx.doi.org/10.15407/rej2021.03.046.

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Subject and Purpose. The elucidation of the molecular mechanisms of action of biomolecules is necessary for the development of state-of-the-art means of diagnosing and treatment. Dielectric studies in the millimeter wave range are effective for puzzling out the nature of the interaction of biomolecules with a surrounding aqueous solvent. Flavin mononucleotide (FMN), which can kill microorganisms and destroy cancer cells, is of particular interest. The aim of the work is to recognize hydration effects (changes in the state of water molecules) in FMN solutions. Methods and Methodology. The compl
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4

Surolia, N., K. Krishnamurthy, and P. R. Adiga. "Enzymic basis of deranged foetal flavin-nucleotide metabolism consequent on immunoneutralization of maternal riboflavin carrier protein in the pregnant rat." Biochemical Journal 230, no. 2 (1985): 363–67. http://dx.doi.org/10.1042/bj2300363.

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A comparison of the kinetic and other parameters of enzymes of flavin-nucleotide metabolism in the whole foetus vis-à-vis the maternal liver in the pregnant rat revealed relatively lower activities of foetal flavokinase and FAD pyrophosphorylase. Passive immunoneutralization of the maternal riboflavin carrier protein suppresses foetal FAD pyrophosphorylase rather selectively. Additionally, although the activities of foetal nucleotide pyrophosphatase and FMN phosphatase were unchanged owing to immunoneutralization, higher activities of these enzymes in the whole foetus as compared with the mate
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5

Brijlal, Sangeetha, A. V. Lakshmi, Mahtab S. Bamji, and P. Suresh. "Flavin metabolism during respiratory infection in mice." British Journal of Nutrition 76, no. 3 (1996): 453–62. http://dx.doi.org/10.1079/bjn19960050.

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Previous control studies carried out in children showed that respiratory infection alters riboflavin metabolism and leads to excessive urinary losses of the vitamin. In order to understand the nature of biochemical changes in riboflavin metabolism during respiratory infection, a study was carried out using the mouse as the experimental model, andKlebsiella pneumonjueas the infective organism. Mice were fed on either a low(0·5 mg/kg)- or high(13·3 mg/kg)-riboflavin semi-synthetic diet. Infection resulted in a 5–6-fold higher excretion of riboflavin in the urine of mice fed on the low-riboflavin
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6

Boniwell, Jeremy M., and Vernon S. Butt. "Flavin Nucleotide-Dependent 3-Hydroxylation of 4-Hydroxyphenylpropanoid Carboxylic Acids by Particulate Preparations from Potato Tubers." Zeitschrift für Naturforschung C 41, no. 1-2 (1986): 56–60. http://dx.doi.org/10.1515/znc-1986-1-210.

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Abstract Particulate preparations from potato tubers, extracted in 4 mᴍ 2-m ercaptoethanol, catalyze the 3-hydroxylation of 4-hydroxyphenylpropanoid carboxylic acids, including p-coumaric acid and tyrosine, in the presence of NADH (or NADPH) and FAD (or FMN); ascorbate could not substitute for these electron donors. Among a range of 4-hydroxylated C6-C2 and C6-C1 compounds tested, only 4-hydroxyphenylacetic acid and p-cresol were hydroxylated. The hydroxylase was sensitive to KCN and diethyldithiocarbam ate and showed some features of phenolase hydroxylation, but no DOPA oxidase nor chlorogeni
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7

Hansen, Sonja, Kim Lewis, and Marin Vulić. "Role of Global Regulators and Nucleotide Metabolism in Antibiotic Tolerance in Escherichia coli." Antimicrobial Agents and Chemotherapy 52, no. 8 (2008): 2718–26. http://dx.doi.org/10.1128/aac.00144-08.

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ABSTRACT Bacterial populations produce a small number of persister cells that exhibit multidrug tolerance. Persister cells are largely responsible for the antibiotic recalcitrance of biofilm infections. The mechanism of persister cell formation largely remains unknown due to the challenges in identifying persister genes. We screened an ordered comprehensive library of 3,985 Escherichia coli knockout strains to identify mutants with altered antibiotic tolerance. Stationary-state cultures in 96-well plates were exposed to ofloxacin at a concentration which allows only tolerant persister cells to
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8

Iwaki, Hiroaki, Stephan Grosse, Hélène Bergeron, et al. "Camphor Pathway Redux: Functional Recombinant Expression of 2,5- and 3,6-Diketocamphane Monooxygenases of Pseudomonas putida ATCC 17453 with Their Cognate Flavin Reductase Catalyzing Baeyer-Villiger Reactions." Applied and Environmental Microbiology 79, no. 10 (2013): 3282–93. http://dx.doi.org/10.1128/aem.03958-12.

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ABSTRACTWhereas the biochemical properties of the monooxygenase components that catalyze the oxidation of 2,5-diketocamphane and 3,6-diketocamphane (2,5-DKCMO and 3,6-DKCMO, respectively) in the initial catabolic steps of (+) and (−) isomeric forms of camphor (CAM) metabolism inPseudomonas putidaATCC 17453 are relatively well characterized, the actual identity of the flavin reductase (Fred) component that provides the reduced flavin to the oxygenases has hitherto been ill defined. In this study, a 37-kDa Fred was purified from a camphor-induced culture ofP. putidaATCC 17453 and this facilitate
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9

Daff, S., M. A. Noble, D. H. Craig, et al. "Control of electron transfer in neuronal NO synthase." Biochemical Society Transactions 29, no. 2 (2001): 147–52. http://dx.doi.org/10.1042/bst0290147.

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The nitric oxide synthases (NOSs) are dimeric flavocytochromes consisting of an oxygenase domain with cytochrome P450-like Cys-ligated haem, coupled to a diflavin reductase domain, which is related to cytochrome P450 reductase. The NOSs catalyse the sequential mono-oxygenation of arginine to N-hydroxyarginine and then to citrulline and NO. The constitutive NOS isoforms (cNOSs) are regulated by calmodulin (CaM), which binds at elevated concentrations of free Ca2+, whereas the inducible isoform binds CaM irreversibly. One of the main structural differences between the constitutive and inducible
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10

Topham, R., M. Goger, K. Pearce, and P. Schultz. "The mobilization of ferritin iron by liver cytosol. A comparison of xanthine and NADH as reducing substrates." Biochemical Journal 261, no. 1 (1989): 137–43. http://dx.doi.org/10.1042/bj2610137.

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Considerable evidence suggests that the release of iron from ferritin is a reductive process. A role in this process has been proposed for two hepatic enzymes, namely xanthine oxidoreductase and an NADH oxidoreductase. The abilities of xanthine and NADH to serve as a source of reducing power for the enzyme-mediated release of ferritin iron (ferrireductase activity) were compared with turkey liver and rat liver homogenates. The maximal velocity (Vmax.) for the reaction with NADH was 50 times greater than with xanthine; however, the substrate concentration required to achieve half-maximal veloci
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