Structure of hen phosvitin: a phosphorus-31 NMR, proton NMR, and laser photochemically induced dynamic nuclear polarization proton NMR study

Vogel, Hans J.

doi:10.1021/bi00272a022

Cited by 42 publications

(34 citation statements)

References 26 publications

(41 reference statements)

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“…Similarly, the chemical shift observed for 5'-adenyl-0-tyrosine is different from that of other phosphodiesters (8, 12, 14). It is not clear why no pKa2 is 28. The data represent the titration data observed for three different groups of the total 125 phosphoserine residues that can be resolved in an 3' P-NMR spectrum.…”

Section: Model Compoundsmentioning

confidence: 95%

Phosphorus-31 nuclear magnetic resonance pH titration studies of the phosphoproteins tropomyosin and glycogen phosphorylase a

Vogel¹,

Bridger²

1983

Can. J. Biochem. Cell Biol.

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31P nuclear magnetic resonance (NMR), pH titration studies of the phosphoproteins tropomyosin and glycogen phosphorylase a (in the presence of the inhibitor glucose) show that the resonances for the phosphoserine regulatory sites shift with pH. Analysis of line widths indicates that both residues have considerable mobility. These results are in agreement with studies on similar phosphorylated sites on other proteins, leading us to propose that mobility is a general feature of such regulatory sites. pH titration studies on a series of model compounds have indicated that an empirical correlation exists between the Hill coefficient n (a measure of the cooperativity of the titration curve) and the presence of charged groups in the vicinity of the phosphoryl moiety. Moreover, these studies showed that within one class of similarly substituted phosphorus compounds the chemical shifts, the titration behaviour, and the pKa2 were comparable and allow for easy identification of these compounds. The pKa2 values for phosphoserine residues of proteins are in general slightly higher than those of phosphomonoester-containing small compounds. The titration data prompt our estimation that the maximal amount of energy associated with a salt linkage between a phosphoseryl side chain and a positively charged group is about 5 kcal (1 cal = 4.1868 J).

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Section: Model Compoundsmentioning

confidence: 95%

Phosphorus-31 nuclear magnetic resonance pH titration studies of the phosphoproteins tropomyosin and glycogen phosphorylase a

Vogel¹,

Bridger²

1983

Can. J. Biochem. Cell Biol.

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“…Model phosvitin stock solutions in D 2 O (6–10 mM phosphoserine) were first qualitatively assessed using 31 P NMR at a magnetic field strength of 16.45 T. In these 31 P NMR spectra, no signals of impurities were observed. As the phosphoserine residues in phosvitin had slightly different chemical and physical surroundings, they are presented as an envelope of signals that appear as an unresolved lineshape at pH 4 (Figure a) …”

Section: Resultsmentioning

confidence: 99%

“…As the phosphoserine residues in phosvitin had slightly different chemical and physical surroundings, they are presented as an envelope of signals that appear as an unresolved lineshape at pH 4 (Figure 2a). [18,19] To verify whether removal of the Fe(III) from the phosvitin complex indeed increased the signal due to the removal of the paramagnetic broadening, an excess of EDTA (>10 mM) was added to the solution. Both line-narrowing and increase in signal integral were observed upon addition of EDTA (Figure 2b).…”

Section: Calculationsmentioning

confidence: 99%

“…Earlier work showed the ability of 31 P NMR to assess the effect of pH on phosvitin . Here, we want to expand on this approach by exploring the applicability of 31 P NMR for assessment of the Fe(III)‐phosvitin binding.…”

Section: Introductionmentioning

confidence: 99%

“…[10] This weaker binding enables Fe(III) to start playing a significant role in lipid oxidation. An effective route to inhibit lipid oxidation in mayonnaise is the removal of iron from the Fe(III)-phosvitin complex by adding a strong chelator such as ethylenediaminetetraacetic acid (EDTA), [13] which has a higher binding strength to Fe(III), log K = 25, [14] than phosvitin (log K = [18][19][20][21]. [15] Other routes to inhibit lipid oxidation involve antioxidants that are hypothesized to either directly interact with the free-radical process or inhibit the activity of pro-oxidants.…”

Section: Introductionmentioning

confidence: 99%

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³¹P NMR assessment of the phosvitin‐iron complex in mayonnaise

Merkx

Delić

Wierenga

et al. 2018

Magnetic Reson in Chemistry

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Lipid oxidation is the main reason for the limited shelf life of mayonnaise. One of the main catalysts of this process is iron, which is introduced in its ferric (Fe(III)) form via phosvitin, an egg yolk phosphoprotein rich in phosphoserines. The binding of Fe(III) to phosvitin and its ability to establish a redox couple with Fe(II) is believed to determine the oxidation rate of unsaturated lipids. In this work, a 31P NMR based method was developed to quantify loading of phosvitin with Fe(III) and its reductive release. Both features could be quantified in model phosvitin solutions by exploiting the paramagnetic broadening of 31P NMR signal of phosphoserine residues by Fe(III). This method was then successfully applied to quantify the phosvitin‐Fe(III) loading in mayonnaise water phase by liquid NMR, whereas 31P NMR MAS could only provide a qualitative measure. The 31P NMR method showed a direct relation between loading of the Fe(III)‐phosvitin complex and lipid oxidation.

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Solution structure of native proteins with irregular folds from Raman optical activity

et al. 2000

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Structure of hen phosvitin: a phosphorus-31 NMR, proton NMR, and laser photochemically induced dynamic nuclear polarization proton NMR study

Cited by 42 publications

References 26 publications

Phosphorus-31 nuclear magnetic resonance pH titration studies of the phosphoproteins tropomyosin and glycogen phosphorylase a

Phosphorus-31 nuclear magnetic resonance pH titration studies of the phosphoproteins tropomyosin and glycogen phosphorylase a

³¹P NMR assessment of the phosvitin‐iron complex in mayonnaise

Solution structure of native proteins with irregular folds from Raman optical activity

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Structure of hen phosvitin: a phosphorus-31 NMR, proton NMR, and laser photochemically induced dynamic nuclear polarization proton NMR study

Cited by 42 publications

References 26 publications

Phosphorus-31 nuclear magnetic resonance pH titration studies of the phosphoproteins tropomyosin and glycogen phosphorylase a

Phosphorus-31 nuclear magnetic resonance pH titration studies of the phosphoproteins tropomyosin and glycogen phosphorylase a

31P NMR assessment of the phosvitin‐iron complex in mayonnaise

Solution structure of native proteins with irregular folds from Raman optical activity

Contact Info

Product

Resources

About

³¹P NMR assessment of the phosvitin‐iron complex in mayonnaise