Results 191 to 200 of about 29,275 (243)
Widespread distribution of BpfA-mediated bisphenol F degradation among members of the Pseudomonadota and Actinomycetota. [PDF]
ISME JZhang M +10 more
europepmc +1 more source
Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts [PDF]
Journal of Biotechnology, 2006 During the last decades a large number of flavin-dependent monooxygenases have been isolated and studied. This has revealed that flavoprotein monooxygenases are able to catalyze a remarkable wide variety of oxidative reactions such as regioselective ...
Willem J H Van Berkel, Marco W Fraaije
exaly +2 more sources
The Oxidation of Thiols by Flavoprotein Oxidases: a Biocatalytic Route to Reactive Thiocarbonyls
Angewandte Chemie - International Edition, 2014 Flavoprotein oxidases are a diverse class of biocatalysts, most of which catalyze the oxidation of C[BOND]O, C[BOND]N, or C[BOND]C bonds. Flavoprotein oxidases that are known to catalyze the oxidation of C[BOND]S bonds are rare, being limited to enzymes ...
Tom A Ewing +2 more
exaly +2 more sources
Systematic Assessment of Uncoupling in Flavoprotein Oxidases and Monooxygenases [PDF]
ACS Sustainable Chemistry and Engineering, 2023 Flavin as a cofactor is an extremely versatile molecule that participates in a wide range of biochemical reactions. A special characteristic of the flavin cofactor, unique for a metal free cofactor, is its ability to react in its reduced form with ...
Marco W Fraaije
exaly +2 more sources
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2003
Flavoproteins are involved in a wide variety of enzymatic reactions like oxidation, reduction and mono-oxygenation. Consequently, flavin cofactors occur in many different forms including, for example, the oxidized semiquinone and reduced states as well as the C4a-(hydro)peroxyflavin form.
Hefti, M., Vervoort, J.
openaire +3 more sources
Flavoproteins are involved in a wide variety of enzymatic reactions like oxidation, reduction and mono-oxygenation. Consequently, flavin cofactors occur in many different forms including, for example, the oxidized semiquinone and reduced states as well as the C4a-(hydro)peroxyflavin form.
Hefti, M., Vervoort, J.
openaire +3 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
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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
The VAO/PCMH flavoprotein family [PDF]
Archives of Biochemistry and Biophysics, 2017 The VAO/PCMH flavoprotein family consists of structurally homologous flavin-dependent enzymes that catalyze a wide range of chemical reactions. Family members share an architecture consisting of a conserved FAD-binding domain and a more variable ...
Tom A Ewing +2 more
exaly +2 more sources