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

Author: Grafiati

Published: 7 June 2025

Last updated: 2 August 2025

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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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11

Wang, Xia, Gang Mi, Cuicui Wang, et al. "Prediction of flavin mono-nucleotide binding sites using modified PSSM profile and ensemble support vector machine." Computers in Biology and Medicine 42, no. 11 (2012): 1053–59. http://dx.doi.org/10.1016/j.compbiomed.2012.08.005.

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12

Bjelosevic, Stefan, Rahel Fauth, Brian T. Do, et al. "Riboflavin Drives Nucleotide Biosynthesis and Iron-Sulfur Metabolism to Promote Acute Myeloid Leukemia." Blood 144, Supplement 1 (2024): 626. https://doi.org/10.1182/blood-2024-208370.

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Cofactors, many of which are vitamin-derived, are organic molecules with diverse biological functions. They are required for many metabolic pathways and enzymatic reactions, and thus can influence cell proliferation and differentiation. Though the role of vitamins in non-malignant contexts is relatively well characterized, their role in carcinogenesis is not well defined. Here, we sought to molecularly characterize how vitamins contribute to oncogenesis in acute myeloid leukemia (AML). We performed vitamin depletion screens in AML cells using culture medium designed to mimic human plasma. Thes

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13

Dr., G. Sri Manjula, D.V. Ramanjaneyulu, E. Muralinath, et al. "Epidemiology, Mechanism of Action, Administration, Adverse Effects, Contraindications, Pathophysiology, Pharmacokinetics, Diagnosis, Differential Diagnosis and Treatment of Riboflavin Deficiency." Research and Reviews: Journal of Holistic Nursing 1, no. 2 (2024): 43–50. https://doi.org/10.5281/zenodo.13831693.

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<em>Riboflavin, vitamin B2, is a heat-stable, water-soluble vitamin that the body </em><em>utilizes particularly for the purpose of metabolism of carbohydrates, fats, and protein into glucose for energy. </em><em>Along with the supplemenatation of energy, this vitamin </em><em>behaves as an antioxidant for the proper functioning of the immune system, healthy skin, and hair. In riboflavin deficiency, macronutrients </em><em>such as fats, carbohydrates, and proteins cannot be digested to </em><em>regulate the body. Riboflavin </em><em>plays an important role regarding development, lactation, phy

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14

Vervoort, Jascha, Basil Britto Xavier, Andrew Stewardson, et al. "AnIn VitroDeletion inribEEncoding Lumazine Synthase Contributes to Nitrofurantoin Resistance in Escherichia coli." Antimicrobial Agents and Chemotherapy 58, no. 12 (2014): 7225–33. http://dx.doi.org/10.1128/aac.03952-14.

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ABSTRACTNitrofurantoin has been used for decades for the treatment of urinary tract infections (UTIs), but clinically significant resistance inEscherichia coliis uncommon. Nitrofurantoin concentrations in the gastrointestinal tract tend to be low, which might facilitate selection of nitrofurantoin-resistant (NIT-R) strains in the gut flora. We subjected two nitrofurantoin-susceptible intestinalE. colistrains (ST540-p and ST2747-p) to increasing nitrofurantoin concentrations under aerobic and anaerobic conditions. Whole-genome sequencing was performed for both susceptible isolates and selected

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15

Da’dara, Akram A., Catherine S. Nation, and Patrick J. Skelly. "Metabolism of FAD, FMN and riboflavin (vitamin B2) in the human parasitic blood fluke Schistosoma mansoni." BMC Infectious Diseases 24, no. 1 (2024). http://dx.doi.org/10.1186/s12879-024-09538-z.

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Abstract Background Schistosomiasis is a parasitic disease caused by trematodes of the genus Schistosoma. The intravascular worms acquire the nutrients necessary for their survival from host blood. Since all animals are auxotrophic for riboflavin (vitamin B2), schistosomes too must import it to survive. Riboflavin is an essential component of the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD); these support key functions of dozens of flavoenzymes. Methods Here, using a combination of metabolomics, enzyme kinetics and in silico molecular analysis, we focus on the bi

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16

Qi, Li, Mengke Shi, Fang-Chao Zhu, Chun-Ang Lian, and Li-Sheng He. "Genomic evidence for the first symbiotic Deferribacterota, a novel gut symbiont from the deep-sea hydrothermal vent shrimp Rimicaris kairei." Frontiers in Microbiology 14 (June 29, 2023). http://dx.doi.org/10.3389/fmicb.2023.1179935.

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The genus Rimicaris is the dominant organism living in hydrothermal vents. However, little research has been done on the functions of their intestinal flora. Here, we investigated the potential functions of Deferribacterota, which is dominant in the intestine of Rimicaris kairei from the Central Indian Ridge. In total, six metagenome-assembled genomes (MAGs) of Deferribacterota were obtained using the metagenomic approach. The six Deferribacterota MAGs (Def-MAGs) were clustered into a new branch in the phylogenetic tree. The six Def-MAGs were further classified into three species, including on

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17

Sarkar, Jagannath. "Genomics of Brevibacterium strains reveal adaptations necessary to acclimatize in different marine environments." June 7, 2024. https://doi.org/10.5281/zenodo.13624149.

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<strong>ABSTRACT</strong> Microbes are ubiquitous throughout the seawater and underlying sediment, which covers the vast region of the earth surface. Strains of different genera under the phylum <em>Actinobacteria</em> are ubiquitous all-over different environments of the earth surfaces. A well-studied aerobic genus, <em>Brevibacterium</em>, under the phylum also found to be omnipresent in both marine and terrestrial environments, ranging from coastal to open ocean. Which raise question, whether marine strains are phylogenetically distinct from others or not, and what are the special genomic a

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