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On the relevance of the flavin binding to human D-amino acid oxidase in Flavins and Flavoproteins
, 2008 CALDINELLI, LAURA +3 more
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Spin Dynamics of Flavoproteins
International Journal of Molecular Sciences, 2023 This short review reports the surprising phenomenon of nuclear hyperpolarization occurring in chemical reactions, which is called CIDNP (chemically induced dynamic nuclear polarization) or photo-CIDNP if the chemical reaction is light-driven. The phenomenon occurs in both liquid and solid-state, and electron transfer systems, often carrying flavins as ...
Jörg Matysik +2 more
exaly +3 more sources
Oxidation of amines by flavoproteins [PDF]
Archives of Biochemistry and Biophysics, 2010 Many flavoproteins catalyze the oxidation of primary and secondary amines, with the transfer of a hydride equivalent from a carbon-nitrogen bond to the flavin cofactor. Most of these amine oxidases can be classified into two structural families, the D-amino acid oxidase/sarcosine oxidase family and the monoamine oxidase family.
Paul F Fitzpatrick
exaly +3 more sources
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The acceptor specificity of flavins and flavoproteins. III. Flavoproteins
Biochimica Et Biophysica Acta - Bioenergetics, 1971Abstract 1. The specificity of flavoproteins towards acceptors has been rather neglected, but an attempt is here made to construct a comparative table of acceptor specificities of those flavoprotein enzymes for which data exist. 2. The acceptor specificity of reduced flavin groups, when combined with apoenzyme proteins, is quite different from that ...
Malcolm Dixon
exaly +2 more sources
2003
Flavoproteins are ubiquitous proteins involved in diverse biological processes ranging from redox catalysis and light emission to DNA repair (1). Based on their function, flavoproteins can be divided into several subclasses including electron transferases, photolyases, synthases, dehydrogenases, disulfide reductases, oxidases, and monooxygenases.
van Berkel, W.J.H. +3 more
openaire +2 more sources
Flavoproteins are ubiquitous proteins involved in diverse biological processes ranging from redox catalysis and light emission to DNA repair (1). Based on their function, flavoproteins can be divided into several subclasses including electron transferases, photolyases, synthases, dehydrogenases, disulfide reductases, oxidases, and monooxygenases.
van Berkel, W.J.H. +3 more
openaire +2 more sources
2011
Current technical and methodical advances in electron paramagnetic resonance (EPR) spectroscopy have proven to be very beneficial for studies of stationary and short-lived paramagnetic states in proteins carrying organic cofactors. In particular, the large number of proteins with flavins as prosthetic groups can be examined splendidly by EPR in all its
Schleicher, Erik, Weber, Stefan
openaire +3 more sources
Current technical and methodical advances in electron paramagnetic resonance (EPR) spectroscopy have proven to be very beneficial for studies of stationary and short-lived paramagnetic states in proteins carrying organic cofactors. In particular, the large number of proteins with flavins as prosthetic groups can be examined splendidly by EPR in all its
Schleicher, Erik, Weber, Stefan
openaire +3 more sources
Turning a monocovalent flavoprotein into a bicovalent flavoprotein by structure-inspired mutagenesis
Bioorganic & Medicinal Chemistry, 2014A recently discovered class of bicovalent flavoproteins is an interesting group of enzymes because of their unusual cofactor binding mode, their open active sites and the bulky substrates they can accept. Through a sequence comparison study we have identified a conserved sequence region in bicovalent flavoproteins that is different from monocovalent ...
Kopacz, Malgorzata M., Fraaije, Marco W.
openaire +3 more sources
Vibrational spectroscopy of flavoproteins
2019The flavin cofactor performs many functions in the cell based on the ability of the isoalloxazine ring to undergo one- or two-electron reduction and form covalent adducts with reactants such as amino acids. In addition, the strong visible absorption of the cofactor is also the basis for flavin-dependent photoreceptors.
James N, Iuliano +2 more
openaire +2 more sources