Results 171 to 180 of about 45,388 (244)

<i>Pseudomonas psychrophila</i> Biofilm Formation Inhibition by Thymol Adaptation. [PDF]

J Agric Food Chem
Caballero Gómez N, Manetsberger J, Terriente-Palacios C, Vallarino JG, Benomar N, Abriouel H.   +5 more
europepmc   +1 more source

Determining large hyperfine interactions of a model flavoprotein in the semiquinone state using pulse EPR (electron paramagnetic resonance) techniques. [PDF]

Magn Reson (Gott)
Martínez JI, Frago S, Medina M, García-Rubio I.   +3 more
europepmc   +1 more source

Flavin and deazaflavin biosynthesis in mycobacteria: relevance to physiology, implications for drug discovery, MR-1 antigenicity, and vaccine development. [PDF]

Front Immunol
Oketade N, Chengalroyen MD, Kain D, Lewinsohn DM, Dobos KM.   +4 more
europepmc   +1 more source

Riboflavin Transporter Deficiency as a Cause of Progressive Encephalopathy. [PDF]

Metabolites
Paprocka J, Karpierz J, Hutny M, Hofman-Hutna J, Dobosz A.   +4 more
europepmc   +1 more source

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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.
Yuxuan, Du, Xinyi, Zhang, Hengwei, Zhang, Rongshuai, Zhu, Zhenqiang, Zhao, Jin, Han, Di, Zhang, Xiaoling, Zhang, Xian, Zhang, Xuewei, Pan, Jiajia, You, Zhiming, Rao   +11 more
openaire   +3 more sources

Flavin Mononucleotide-Binding Fluorescent Proteins

Encyclopedia of Biophysics, 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

Ultrafast 2D-IR spectroelectrochemistry of flavin mononucleotide

The Journal of Chemical Physics, 2015
We demonstrate the coupling of ultrafast two-dimensional infrared (2D-IR) spectroscopy to electrochemistry in solution and apply it to flavin mononucleotide, an important cofactor of redox proteins. For this purpose, we designed a spectroelectrochemical cell optimized for 2D-IR measurements in reflection and measured the time-dependent 2D-IR spectra of
Youssef, El Khoury, Luuk J G W, Van Wilderen, Jens, Bredenbeck   +2 more
openaire   +3 more sources

Bacterial Flavin Mononucleotide Riboswitches as Targets for Flavin Analogs

Methods in molecular biology, 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   +3 more sources

Shining light on flavin mononucleotide

Nature Chemistry
Qinglong Shi, Juntao Ye
openaire   +3 more sources

The ins and outs of the flavin mononucleotide cofactor of respiratory complex I

IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology, 2022
The flavin mononucleotide (FMN) cofactor of respiratory complex I occupies a key position in the electron transport chain. Here, the electrons coming from NADH start the sequence of oxidoreduction reactions, which drives the generation of the proton ...
Andrea Curtabbi, J. Enríquez
semanticscholar   +1 more source