Results 151 to 160 of about 10,776 (205)

Direct evolution of riboflavin kinase significantly enhance flavin mononucleotide synthesis by design and optimization of flavin mononucleotide riboswitch

Bioresource Technology, 2023
Flavin mononucleotide (FMN) is the active form of riboflavin. It has a wide range of application scenarios in the pharmaceutical and food additives. However, there are limitations in selecting generic high-throughput screening platforms that improve the properties of enzymes.
Hengwei Zhang, Rongshuai Zhu, Zhenqiang Zhao   +2 more
exaly   +3 more sources

Flavin Mononucleotide-Binding Fluorescent Proteins

, 2013
Flavin mononucleotide (FMN)-binding fluorescent proteins (FbFPs) are novel reporters for cell microscopy, outperforming green fluorescent proteins (GFP) and derivatives in anaerobic or microaerobic environments (Figure 1). Furthermore they are better suited for incorporation into small-sized genomes and for following viral infections, protein ...
LOSI, Aba, VIAPPIANI, Cristiano
openaire   +4 more sources

Optical properties of flavin mononucleotide: A QM/MM study of protein environment effects

Chemical Physics, 2011
We investigate the optical properties of flavin mononucleotide (FMN) as chromophore of a bacterial protein. FMN is studied both in the oxidized and anionic state, by combining hybrid quantum mechanics/molecular mechanics (QM/MM) dynamics with time ...
Elena Cannuccia, Olivia Pulci, Rodolfo Del Sole   +2 more
exaly   +2 more sources

Reversible dissociation of flavin mononucleotide from the mammalian membrane‐bound NADH:ubiquinone oxidoreductase (complex I)

FEBS Letters, 2007
Conditions for the reversible dissociation of flavin mononucleotide (FMN) from the membrane-bound mitochondrial NADH:ubiquinone oxidoreductase (complex I) are described. The catalytic activities of the enzyme, i.e.
Vera G Grivennikova, Gary Cecchini, Andrei D Vinogradov   +2 more
exaly   +2 more sources

Mechanisms of reactions of flavin mononucleotide triplet with aromatic amino acids

Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 2002
Chemical reactions between the photoexcited triplet state of flavin mononucleotide and the aromatic amino acids, N-acetyl tryptophan (TrpH), N-acetyl tyrosine (TyrOH), and N-acetyl histidine (HisH) in aqueous solution have been studied in the pH range 2 ...
Yu P Tsentalovich, P J Hore, R Z Sagdeev   +2 more
exaly   +2 more sources

Flavin mononucleotide reductase of luminous bacteria

Molecular and Cellular Biochemistry, 1975
NAD(P)H: FMN oxidoreductase (flavin reductase) couples in vitro to bacterial luciferase. This reductase, which is also postulated to supply reduced flavin mononucleotide in vivo as a substrate for the bioluminescent reaction, has been partially purified and characterized from two species of luminous bacterial.
W, Duane, J W, Hastings
openaire   +2 more sources

Analysis of the reduction of nitroxides by flavin mononucleotide

Biochimica et Biophysica Acta (BBA) - General Subjects, 1990
This article describes a simple method to prepare hydroxylamines from nitroxides by photo-activated flavin mononucleotide. The half-time of reduction varied from 2 to 38.4 s for a series of nitroxides. For most nitroxides short exposures to light (min) were sufficient to produce significant amounts of hydroxylamine; longer periods of exposure increased
P D, Morse, E K, Ruuge, M J, Petro, H M, Swartz   +3 more
openaire   +2 more sources

The enthalpy of oxidation of flavin mononucleotide

Archives of Biochemistry and Biophysics, 1974
Abstract The oxidation enthalpy of reduced flavin mononucleotide at pH 7.0 in 0.2 m phosphate buffer has been studied by determining the heat associated with the reaction: FMNH 2 + 2 Fe(CN) −3 6 ⇌ FMN + 2 Fe(CN) −4 6 + 2 H + . (a) (The quinone, semiquinone, and hydroquinone forms of FMN are represented as FMN, FMNH, and FMNH 2 , respectively.)
Norman V. Beaudette, Neal Langerman
openaire   +1 more source

Bacterial Flavin Mononucleotide Riboswitches as Targets for Flavin Analogs

2013
Roseoflavin is a toxic riboflavin (vitamin B2) analog and naturally is produced by Streptomyces davawensis. Roseoflavin is converted to roseoflavin mononucleotide (RoFMN) by promiscuous flavokinases (EC 2.7.1.26). Flavin mononucleotide (FMN) riboswitches control the expression of genes involved in riboflavin biosynthesis and/or transport.
Danielle Biscaro, Pedrolli, Matthias, Mack   +1 more
openaire   +2 more sources