Results 1 to 10 of about 7,181 (257)
Reduced Molecular Flavins as Single-Electron Reductants after Photoexcitation
Journal of the American Chemical Society, 2022 Flavoenzymes mediate a multitude of chemical reactions and are catalytically active both in different oxidation states and in covalent adducts with reagents.
Erling Thyrhaug +2 more
exaly +3 more sources
Expanding the chemical space of flavins with pentacyclic architecture. [PDF]
Nat CommunInspired by the prominent redox and optical properties of natural flavins, synthetic flavins have found broad applications in organic, photochemical, and biochemical research. Tailoring these properties of flavins, however, remains a challenge.
Seo D +7 more
europepmc +2 more sources
Flavins and Flavoproteins in the Neuroimmune Landscape of Stress Sensitization and Major Depressive Disorder. [PDF]
J Inflamm ResMatt Scott Schrier,1 Maria Igorevna Smirnova,2– 4 Daniel Paul Nemeth,1 Richard Carlton Deth,5 Ning Quan1,3 1Department of Biomedical Science, Charles E.
Schrier MS +4 more
europepmc +2 more sources
New Phytologist, 2016 13 Pags.- 10 Figs.Iron (Fe) is abundant in soils but generally poorly soluble. Plants, with the exception of Graminaceae, take up Fe using an Fe(III)-chelate reductase coupled to an Fe(II) transporter.
Juan J Rios +2 more
exaly +2 more sources
Photo-CIDNP of Solvent-Exposed Flavins in Flavoproteins. [PDF]
J Phys Chem LettPhotochemically induced dynamic nuclear polarization (photo-CIDNP) is a hyperpolarization NMR technique that enhances the resonances of molecules involved in the formation of spin-correlated radical pairs.
Schmidt A +5 more
europepmc +2 more sources
Journal of the American Chemical Society, 2023 Most flavin-dependent enzymes contain a dissociable flavin cofactor. We present a new approach for installing in vivo a covalent bond between a flavin cofactor and its host protein. By using a flavin transferase and carving a flavinylation motif in target proteins, we demonstrate that "dissociable" flavoproteins can be turned into covalent ...
Yapei Tong +5 more
openaire +3 more sources
Natural Flavins: Occurrence, Role, and Noncanonical Chemistry [PDF]
, 2021 Flavoproteins are of key importance to all life on earth for both primary and secondary metabolism. Most flavin-dependent enzymes utilize flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) as redox cofactor for single-electron and hydride ...
Marco W. Fraaije +4 more
core +1 more source
ChemBioChem, 2022 AbstractMethods for facile site‐selective modifications of proteins are in high demand. We have recently shown that a flavin transferase can be used for site‐specific covalent attachment of a chromo‐ and fluorogenic flavin (FMN) to any targeted protein. Although this Flavin‐tag method resulted in efficient labeling of proteins in vitro, labelling in E.
Yapei Tong +2 more
openaire +3 more sources
Flavin oxidation in flavin‐dependent N‐monooxygenases [PDF]
Protein Science, 2018 AbstractSiderophore A (SidA) from Aspergillus fumigatus is a flavin‐containing monooxygenase that hydroxylates ornithine (Orn) at the amino group of the side chain. Lysine (Lys) also binds to the active site of SidA; however, hydroxylation is not efficient and H2O2 is the main product.
Sobrado, Pablo +3 more
openaire +3 more sources
Regulation of the Flavin Redox Potential by Flavin‐Binding Antibodies [PDF]
European Journal of Biochemistry, 1997 Single‐chain Fv antibody fragments binding different flavin forms [10‐(5'‐carboxybutyl‐)flavin (Flox) and 10‐(5'‐carboxybutyl)‐1,5‐dihydroflavin (Flred)] have been generated from an antibody phage‐display library to study how a protein environment regulates the redox potential, starting from a protein other than a natural flavoprotein.
Bruggeman, Y.E. +6 more
openaire +2 more sources