Results 171 to 180 of about 11,677 (208)
Electron-Transferring Flavoprotein and Its Dehydrogenase Required for Fungal Pathogenicity in Arthrobotrys oligospora. [PDF]
Int J Mol SciLiu Y, Li Z, Liu J, Zhang X, Wang X.
europepmc +1 more source
Assessing the potential of deep learning for protein-ligand docking. [PDF]
Nat Mach IntellMorehead A +4 more
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Illuminating the dark majority: photobiology of nonphotosynthetic bacteria. [PDF]
Photochem Photobiol SciCianflone E, Paternò GM.
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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
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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
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.
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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.
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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
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
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Biochemistry, 1985
The oxidative half-reaction of electron-transfer flavoprotein (ETF), electron transfer from ETF to electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO), is dependent on complementary surface charges on the two proteins. ETF is the positively charged member of the redox pair.
J D, Beckmann, F E, Frerman
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The oxidative half-reaction of electron-transfer flavoprotein (ETF), electron transfer from ETF to electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO), is dependent on complementary surface charges on the two proteins. ETF is the positively charged member of the redox pair.
J D, Beckmann, F E, Frerman
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Riboflavin-Binding Protein (Flavoprotein)
2007absent
Guérin-Dubiard, Catherine +2 more
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