Results 151 to 160 of about 26,547 (202)

NMR of Flavoproteins

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

Flavoprotein Kinetics

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

Methyl rotors in flavoproteins

Phys. Chem. Chem. Phys., 2014
ENDOR evidence shows that methyl groups in flavin behave as quantum locked rotors.
Jesús I. Martínez   +3 more
openaire   +3 more sources

Radicals in Flavoproteins

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

The acceptor specificity of flavins and flavoproteins. III. Flavoproteins

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1971
Abstract 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 ...
openaire   +1 more source

Turning a monocovalent flavoprotein into a bicovalent flavoprotein by structure-inspired mutagenesis

Bioorganic & Medicinal Chemistry, 2014
A 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

2019
The 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

Substrate Dehydrogenation by Flavoproteins

Accounts of Chemical Research, 2001
Enzymes with tightly bound FMN or FAD as cofactor catalyze the oxidation of a wide range of substrates. The chemical versatility of the isoalloxazine ring provides these enzymes with a range of potential mechanisms. Recent progress in elucidating the mechanisms of oxidation of organic substrates by flavoenzymes is described, focusing on the oxidation ...
openaire   +2 more sources

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