Proton NMR study of the interaction of riboflavin with the egg‐yolk apoprotein

Lubas, Barbara; Sołtysik, Mariusz; Steczko, Janusz; Ostrowski, W

doi:10.1016/0014-5793(77)80378-5

Cited by 8 publications

(1 citation statement)

References 17 publications

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“…Another unique characteristic of the three chicken RfBPs is the presence of nine disulfide bridges, whose assignment was made chemically in the egg white protein (Hamazume et al ., 1987), that play an important structural role since refolding of the molecule is fast and efficient when denaturation is carried out, leaving them intact (McClelland et al ., 1995). The interactions of the chicken RfBPs with different flavin derivatives are probably the best studied of any flavoprotein (Lubas et al ., 1977; Walsh et al ., 1978; Nishina et al ., 1980; Becvar and Palmer, 1982; Matsui et al ., 1982; Wessiak et al ., 1984). Upon binding to the chicken RfBPs, riboflavin loses its characteristic fluorescence, a fact interpreted as due to a stacking of the isoalloxazine ring of the vitamin with aromatic side chains of the protein molecule (Blankenhorn, 1978).…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of chicken riboflavin-binding protein

1997

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play an essential role in the survival of the fetus.The family of the chicken RfBPs includes three wellThe crystal structure of chicken egg white riboflavinknown proteins that are the product of the same gene but binding protein, determined to a resolution of 2.5 Å, have undergone different post-translational modifications is the prototype of a family that includes other ribo- (White and Merrill, 1988). The proteins can be purified flavin-and folate-binding proteins. An unusual characfrom egg white (Rhodes et al., 1959), egg yolk (Ostrowski teristic of these molecules is their high degree of cross et al., 1962) and from the plasma of laying hens (Miller linking by disulfide bridges and, in the case of the et al., 1982a). Egg white RfBP is synthesized by the avian proteins, the presence of stretches of highly oviduct cells (Mandeles and Ducay, 1962), plasma RfBP phosphorylated polypeptide chain. The structure of is produced in the liver under estrogen control and yolk chicken egg white riboflavin-binding protein is characRfBP is the result of a proteolytic cleavage of the last terized by a ligand-binding domain and a phosphoryl-11-13 amino acids of plasma RfBP when the molecule ated motif. The ligand-binding domain has a fold that crosses the oocyte membrane (Norioka et al., 1985). The appears to be strongly conditioned by the presence three proteins have a single binding site for riboflavin of the disulfide bridges. The phosphorylated motif, with a dissociation constant of 1.3 nM in the pH range essential for vitamin uptake, is made up of two helices 6-9; removal of the vitamin from the holoprotein is found before and after the flexible phosphorylated accomplished at lower pH where the affinity for the region. The riboflavin molecule binds to the protein specific ligand is substantially reduced (Müller and van with the isoalloxazine ring stacked in between the rings Berkel, 1991

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Section: Introductionmentioning

confidence: 99%

Crystal structure of chicken riboflavin-binding protein

1997

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NMR Spectroscopy on Flavins and Flavoproteins

Müller¹

2014

Methods in Molecular Biology

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(1)H-, (11)B-, (13)C-, (15)N-, (17)O-, (19)F-, and (31)P-NMR chemical shifts of flavocoenzymes and derivatives of it, as well as of alloxazines and isoalloxazinium salts, from NMR experiments performed under various experimental conditions (e.g., dependence of the chemical shifts on temperature, concentration, solvent polarity, and pH) are reported. Also solid-state (13)C- and (15)N-NMR experiments are described revealing the anisotropic values of corresponding chemical shifts. These data, in combination with a number of coupling constants, led to a detailed description of the electronic structure of oxidized and reduced flavins. The data also demonstrate that the structure of oxidized flavin can assume a configuration deviating from coplanarity, depending on substitutions in the isoalloxazine ring, while that of reduced flavin exhibits several configurations, from almost planar to quite bended. The complexes formed between oxidized flavin and metal ions or organic molecules revealed three coordination sites with metal ions (depending on the chemical nature of the ion), and specific interactions between the pyrimidine moiety of flavin and organic molecules, mimicking specific interactions between apoflavoproteins and their coenzymes. Most NMR studies on flavoproteins were performed using (13)C- and (15)N-substituted coenzymes, either specifically enriched in the pterin moiety of flavin or uniformly labeled flavins. The chemical shifts of free flavins are used as a guide in the interpretation of the chemical shifts observed in flavoproteins. Although the hydrogen-bonding pattern in oxidized and reduced flavoproteins varies considerably, no correlation is obvious between these patterns and the corresponding redox potentials. In all reduced flavoproteins the N(1)H group of the flavocoenzyme is deprotonated, an exception is thioredoxin reductase. Three-dimensional structures of only a few flavoproteins, mostly belonging to the family of flavodoxins, have been solved. Also the kinetics of unfolding and refolding of flavodoxins has been investigated by NMR techniques. In addition, (31)P-NMR data of all so far studied flavoproteins and some (19)F-NMR spectra are discussed.

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Calorimetric studies of flavin-binding proteins: FMN and FAD binding to hen egg riboflavin-binding proteins

Nowak¹,

Langerman²

1982

Archives of Biochemistry and Biophysics

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Proton NMR study of the interaction of riboflavin with the egg‐yolk apoprotein

Cited by 8 publications

References 17 publications

Crystal structure of chicken riboflavin-binding protein

Crystal structure of chicken riboflavin-binding protein

NMR Spectroscopy on Flavins and Flavoproteins

Calorimetric studies of flavin-binding proteins: FMN and FAD binding to hen egg riboflavin-binding proteins

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