Periodate oxidation of methionine in proteins

Yamasaki, Ryohei; Osuga, David T.; Feeney, Robert E.

doi:10.1016/0003-2697(82)90127-0

Cited by 45 publications

(35 citation statements)

References 28 publications

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“…Although the possible oxidation of tryptophan and cysteine residues cannot be excluded by these studies, no other amino acid appeared to react under the conditions used. These data are in agreement with the results of other studies, which have shown that, under certain conditions, methionine residues may be more readily oxidized than other amino acids such as tryptophan, tyrosine, and histidine (3,31). It is, therefore, possible that the interaction of the oxidizing reagents with methionine residues in proteins may be a significant cause of the dysfunctions observed in neutrophils that have undergone a respiratory burst (19-23, 36, 37).…”

supporting

confidence: 91%

“…1 and 2). Despite indications that sulfoxidation of methionine may occur frequently under physiological conditions, the importance of this reaction remains largely unrecognized (3). The absence of a rapid facile assay for the detection of methionine sulfoxide [Met(O)] residues in proteins has hindered studies in this area.…”

mentioning

confidence: 99%

“…Although the oxidation of methionine residues does not always result in protein inactivation (3,38), significant reduction in biological activity has been observed with numerous proteins (1,2). In these studies, three enzymes, lysozyme, lactate dehydrogenase, and Met(O)-peptide reductase, were partially inactivated in PMA-treated neutrophils.…”

mentioning

confidence: 99%

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Oxidation of methionine residues in proteins of activated human neutrophils.

Fliss¹,

Weissbach²,

Brot³

1983

Proc. Natl. Acad. Sci. U.S.A.

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A simple assay for the detection of 35S-labeled methionine sulfoxide residues in proteins is described. The assay, which is based on the ability of CNBr to react with methionine but not with methionine sulfoxide, requires the prelabeling of cellular proteins with [3S]methionine. The assay was used to study the extent of methionine oxidation in newly synthesized proteins of both activated and quiescent human neutrophils. In cells undergoing a phorbol 12-myristate 13-acetate-induced respiratory burst, about 66% of all methionine residues in newly synthesized proteins were oxidized to the sulfoxide derivative, as compared with 9% in cells not treated with the phorbol ester. In contrast, quantitation of methionine sulfoxide content in the total cellular protein by means of amino acid analysis showed that only 22% of all methionine residues were oxidized in activated cells as compared with 9% in quiescent cells. It is proposed that methionine residues in nascent polypeptide chains are more susceptible to oxidation than those in completed proteins.Methionine residues in proteins can readily be oxidized to the sulfoxide derivative in the presence of suitable oxidizing reagents, a reaction that can result in the inactivation of certain proteins (for reviews, see refs. 1 and 2). Despite indications that sulfoxidation of methionine may occur frequently under physiological conditions, the importance of this reaction remains largely unrecognized (3). The absence of a rapid facile assay for the detection of methionine sulfoxide [Met(O)] residues in proteins has hindered studies in this area. Because Met(O) is unstable to acid hydrolysis (4), long and tedious methods, involving alkaline hydrolysis or alkylation of methionine, are normally used (5). The present report describes a simple assay for the detection of Met(O) residues in proteins labeled with [3S]-methionine. The assay, which is based on the ability of CNBr to react with methionine but not with methionine sulfoxide (6), was used to examine the oxidation of methionine residues in human neutrophils. Neutrophils were chosen for these studies because of their ability to produce copious quantities of oxidizing reagents on activation. As part of their microbicidal response, neutrophils can be activated by a variety of agents such as chemotactic peptides, complement, insoluble particles, and others (7). The activated cells undergo a respiratory burst during which they produce oxidizing reagents such as superoxide anion (O°), hydrogen peroxide (H202), hydroxyl radicals, and hypochlorite ions (8-10), which are highly toxic to extracellular microorganisms and tissues (9, 11-13). These reagents can also inactivate chemotactic peptides and other polypeptides through selective oxidation of methionine residues (14-18). Recently, it has become apparent that the indiscriminate release of these oxy-radicals can damage the neutrophils themselves. Several studies have shown that the respiratory burst can lead to a decrease in neutrophil function through autooxidation (19)(20...

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supporting

confidence: 91%

mentioning

confidence: 99%

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Oxidation of methionine residues in proteins of activated human neutrophils.

Fliss¹,

Weissbach²,

Brot³

1983

Proc. Natl. Acad. Sci. U.S.A.

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“…[19][20][21][22][23] Recently, Ondracek et al 24 also reported the structure-function relationships of lysozyme with periodate. In view of the widespread use of periodate in protein modification, the mechanism of periodate oxidizing certain amino acids in lysozyme is not clear up to now.…”

Section: Possible Mechanism Of the Reactionmentioning

confidence: 99%

“…The product of the reaction between periodate and lysozyme did not react with luminol chemiluminescently. Feeney 19,20 and De la Llosa 21 reported that periodate could oxidize the methionine in proteins. Therefore, it may be concluded that methionine in lysozyme reacted with periodate.…”

Section: Possible Mechanism Of the Reactionmentioning

confidence: 99%

A New Analytical Procedure for Assay of Lysozyme in Human Tear and Saliva with Immobilized Reagents in Flow Injection Chemiluminescence System

Song

Hou

2003

ANAL. SCI.

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Oxidative Folding of Peptides with Cystine‐Knot Architectures: Kinetic Studies and Optimization of Folding Conditions

Reinwarth¹,

Glotzbach²,

Tomaszowski³

et al. 2012

ChemBioChem

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Bioactive peptides often contain several disulfide bonds that provide the main contribution to conformational rigidity and structural, thermal, or biological stability. Among them, cystine-knot peptides-commonly named "knottins"-make up a subclass with several thousand natural members. Hence, they are considered promising frameworks for peptide-based pharmaceuticals. Although cystine-knot peptides are available through chemical and recombinant synthetic routes, oxidative folding to afford the bioactive isomers still remains a crucial step. We therefore investigated the oxidative folding of ten protease-inhibiting peptides from two knottin families, as well as that of an HIV entry inhibitor and of aprotinin, under two conventional sets of folding conditions and by a newly developed procedure. Kinetic studies identified folding conditions that resulted in correctly folded miniproteins with high rates of conversion even for highly hydrophobic and aggregation-prone peptides in concentrated solutions.

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Periodate oxidation of methionine in proteins

Cited by 45 publications

References 28 publications

Oxidation of methionine residues in proteins of activated human neutrophils.

Oxidation of methionine residues in proteins of activated human neutrophils.

A New Analytical Procedure for Assay of Lysozyme in Human Tear and Saliva with Immobilized Reagents in Flow Injection Chemiluminescence System

Oxidative Folding of Peptides with Cystine‐Knot Architectures: Kinetic Studies and Optimization of Folding Conditions

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