Spectroscopic and magnetic studies of iron(III) phosvitins

Webb, James L. A.; Multani, Jagir S.; Saltman, Paul; Beach, Nancy A.; Gray, Harry B.

doi:10.1021/bi00733a021

Cited by 47 publications

(29 citation statements)

References 18 publications

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“…The values of the hyperfine parameters, summarised in Table 3, clearly indicated that iron is present in milk as high-spin Fe 3þ ions in a distorted octahedral configuration. This is in total contradiction with tetrahedral configuration assumed from spectral analysis of iron fortified milk and Fe-phosvitin complex (Carmichael et al, 1975;Gaucheron, 2000;Gaucheron et al, 1997;Hegenauer, Saltman, Ludwig, et al, 1979;Webb et al, 1973). Nevertheless, Webb et al (1973) reported an octahedral coordination structure in Fe-phosvitin complexes set aside by scientists working on milk iron fortification.…”

Section: Fe Mössbauer Studymentioning

confidence: 78%

“…This is in total contradiction with tetrahedral configuration assumed from spectral analysis of iron fortified milk and Fe-phosvitin complex (Carmichael et al, 1975;Gaucheron, 2000;Gaucheron et al, 1997;Hegenauer, Saltman, Ludwig, et al, 1979;Webb et al, 1973). Nevertheless, Webb et al (1973) reported an octahedral coordination structure in Fe-phosvitin complexes set aside by scientists working on milk iron fortification. Hegenauer, Saltman, and Nace (1979) succinctly mentioned an octahedral coordination structure less compatible with protein-Fe binary complexes than with protein-Fe-ligand ternary complexes.…”

Section: Fe Mössbauer Studymentioning

confidence: 78%

“…It is widely assumed that iron is chelated with phosphoseryl residues in caseins and would adopt a tetrahedral structure as observed with ferric iron saturated phosvitin. Nevertheless, study of iron saturated phosvitin also shows that iron is linked by phosvitin phosphoseryl residues in an octahedral coordination (Webb, Multani, Saltman, Beach, & Gray, 1973).…”

Section: Introductionmentioning

confidence: 99%

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Iron fortification of skim milk: Minerals and 57Fe Mössbauer study

Raouche¹,

Naille²,

Dobenesque³

et al. 2009

International Dairy Journal

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Section: Fe Mössbauer Studymentioning

confidence: 78%

Section: Fe Mössbauer Studymentioning

confidence: 78%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Iron fortification of skim milk: Minerals and 57Fe Mössbauer study

Raouche¹,

Naille²,

Dobenesque³

et al. 2009

International Dairy Journal

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“…However, its potential binding capacity is much higher (about 60 atoms per molecule). 9,10) The bound iron is not easily released, even by the high temperature treatment of autoclaving.…”

mentioning

confidence: 99%

Egg Yolk Phosvitin Inhibits Hydroxyl Radical Formation from the Fenton Reaction

Ishikawa

Yano

Arihara

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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Phosvitin, a phosphoprotein known as an iron-carrier in egg yolk, binds almost all the yolk iron. In this study, we investigated the effect of phosvitin on Fe(II)-catalyzed hydroxyl radical ( OH) formation from H 2 O 2 in the Fenton reaction system. Using electron spin resonance (ESR) with 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) and deoxyribose degradation assays, we observed by both assays that phosvitin more effectively inhibited OH formation than iron-binding proteins such as ferritin and transferrin. The effectiveness of phosvitin was related to the iron concentration, indicating that phosvitin acts as an antioxidant by chelating iron ions. Phosvitin accelerates Fe(II) autoxidation and thus decreases the availability of Fe(II) for participation in the OH-generating Fenton reaction. Furthermore, using the plasmid DNA strand breakage assay, phosvitin protected DNA against oxidative damage induced by Fe(II) and H 2 O 2 . These results provide insight into the mechanism of protection of the developing embryo against iron-dependent oxidative damage in ovo.

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“…1) using trypsin, the undecapeptide has provided a useful starting point for the interpretation of the dichroic spectra of haem proteins [6,7]. The NMR method of Evans [8], described below, has proved ideal for solution studies of the magnetic behaviour of metal centres in proteins [9]. The present paper describes the use of this method to investigate the pH-dependence of the magnetic moment of the ferric form of the undecapeptide.…”

mentioning

confidence: 99%

Magnetic Studies on the Ferri‐haem Undecapeptide of Cytochrome c

Jehanli

Stotter

Wilson

1976

European Journal of Biochemistry

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The pH-dependence of the magnetic moment of a ferri-haem undecapeptide, produced by peptic digestion of cytochrome c, has been measured in aqueous solution using a nuclear magnetic resonance method.Below pH 3 the magnetic moment is consistent with the p.resence of hydroxo-bridged dimers of high-spin iron(II1). Above pH 7 the iron(II1) is low-spin, the spin crossover conforming to a simple titration curve with pK 6.3 (n = 1). This transition is discussed with reference to spectrophotometric studies of ligand binding at the haem.The influence of the protein on the metal ion at the active site of a metalloenzyme is central to the theory of entasis [l]. The influence of globin on haem has been studied using the properties of intact haemoglobin [2], while iron-sulphur proteins have been approached in a complimentary manner by studying the effects of binding small peptides to their chemically synthesized iron-sulphur cores [3]. An intermediate approach, which we are beginning to investigate, is to make use of metal-containing peptide fragments resulting from the enzymic digestion of native enzymes.Of particular interest is a haem-containing undecapeptide ( Fig. 1) derived from peptic hydrolysis of cytochrome c [4]. This provides an opportunity to study the haem group in aqueous solution relatively unshielded by protein, yet soluble over an appreciable pH range. In addition, only a limited number of donor groups may be expected to interact with

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Spectroscopic and magnetic studies of iron(III) phosvitins

Cited by 47 publications

References 18 publications

Iron fortification of skim milk: Minerals and 57Fe Mössbauer study

Iron fortification of skim milk: Minerals and 57Fe Mössbauer study

Egg Yolk Phosvitin Inhibits Hydroxyl Radical Formation from the Fenton Reaction

Magnetic Studies on the Ferri‐haem Undecapeptide of Cytochrome c

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