Key role of cysteine residues and sulfenic acids in thermal- and H2O2-mediated modification of β-lactoglobulin

Krämer, Anna C.; Thulstrup, Peter W.; Lund, Marianne N.; Davies, Michael J.

doi:10.1016/j.freeradbiomed.2016.07.010

Cited by 34 publications

(56 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Traditional amino acid analysis with performic acid oxidation as a sample pretreatment for the determination of methionine or cysteine may overestimate these amino acids; if the reduced and the oxidized form(s) are originally present in a sample, oxidation will not permit detection because both forms are oxidized to the same analyte . The analysis of free thiols can be valuable in this case …”

Section: Discussionmentioning

confidence: 99%

“…Further one‐ and two‐electron oxidations at the cysteine sulfur atom lead to cysteine sulfenic ( 55 ), sulfinic ( 56 ), and sulfonic ( 57 ) acids as well as the respective radical intermediates . Cysteine sulfenic acid was detected in H 2 O 2 ‐oxidized β‐lactoglobulin …”

Section: Radical Reactions On Proteinsmentioning

confidence: 99%

“…In this context, however, it is necessary to mention that the disappearance of thiol groups does not necessarily imply oxidation because thiols can also participate in Maillard reactions . The sulfenic acid ( 55 ) as a further cysteine oxidation product was identified after oxidation of β‐lactoglobulin with hydrogen peroxide in a model system …”

Section: Analysis Of Protein Oxidation In Foodmentioning

confidence: 99%

See 2 more Smart Citations

The Chemistry of Protein Oxidation in Food

2019

View full text Add to dashboard Cite

Oxidation is one of the deterioration reactions of proteins in food, the importance of which is comparable to others such as Maillard, lipation, or protein‐phenol reactions. While research on protein oxidation has led to a precise understanding of the processes and consequences in physiological systems, knowledge about the specific effects of protein oxidation in food or the role of “oxidized” dietary protein for the human body is comparatively scarce. Food protein oxidation can occur during the whole processing axis, from primary production to intestinal digestion. The present review summarizes the current knowledge and mechanisms of food protein oxidation from a chemical, technological, and nutritional–physiological viewpoint and gives a comprehensive classification of the individual reactions. Different analytical approaches are compared, and the relationship between oxidation of food proteins and oxidative stress in vivo is critically evaluated.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Radical Reactions On Proteinsmentioning

confidence: 99%

Section: Analysis Of Protein Oxidation In Foodmentioning

confidence: 99%

See 1 more Smart Citation

The Chemistry of Protein Oxidation in Food

2019

View full text Add to dashboard Cite

show abstract

“…The reaction pH (7.4) was maintained using sodium phosphate buffer (0.1 M). Subsequently excess GSH and salt were removed using a PD10 column, and the samples incubated for 30 min with dimedone (5 mM, from a stock solution in 95% ethanol), before analysis by LC-MS/MS as described previously [55]. Briefly, 10 μg of the protein was dried down in a SpeedVac RVC 2-33 (Christ, Germany), denaturated using 8 M urea, reduced with 40 mM DTT for 45 min, and alkylated with iodoacetamide (77 mM) for 60 min in the dark.…”

Section: Experimental Methodsmentioning

confidence: 99%

Protein cysteine oxidation in redox signaling: Caveats on sulfenic acid detection and quantification

Forman

Davies

Krämer

et al. 2017

Archives of Biochemistry and Biophysics

Self Cite

View full text Add to dashboard Cite

Oxidation of critical signaling protein cysteines regulated by H2O2 has been considered to involve sulfenic acid (RSOH) formation. RSOH may subsequently form either a sulfenyl amide (RSNHR’) with a neighboring amide, or a mixed disulfide (RSSR’) with another protein cysteine or glutathione. Previous studies have claimed that RSOH can be detected as an adduct (e.g., with 5,5-dimethylcyclohexane-1,3-dione; dimedone). Here, kinetic data are discussed which indicate that few proteins can form RSOH under physiological signaling conditions. We also present experimental evidence that indicates that (1) dimedone reacts rapidly with sulfenyl amides, and more rapidly than with sulfenic acids, and (2) that disulfides can react reversibly with amides to form sulfenyl amides. As some proteins are more stable as the sulfenyl amide than as a glutathionylated species, the former may account for some of the species previously identified as the “sulfenome” - the cellular complement of reversibly-oxidized thiol proteins generated via sulfenic acids.

show abstract

“…Weitere Ein‐ oder Zwei‐Elektronen‐Oxidationen am Schwefelatom von Cystein führen zu den entsprechenden Sulfen‐ 55 , Sulfin‐ 56 und Sulfonsäuren 57 sowie den radikalischen Intermediaten . Die Sulfensäure 55 wurde in H 2 O 2 ‐oxidiertem β‐Lactoglobulin nachgewiesen …”

Section: Radikalische Reaktionen An Proteinenunclassified

Die Chemie der Proteinoxidation in Lebensmitteln

Hellwig

2019

Angewandte Chemie

View full text Add to dashboard Cite

Die Oxidation ist eine der Abbaureaktionen von Proteinen in Lebensmitteln, deren Bedeutung nicht hinter der von anderen wie der Maillard‐Reaktion, Lipierung oder Protein‐Phenol‐Reaktionen zurückbleibt. Während die Untersuchung der Proteinoxidation zu einem vertieften Verständnis der Prozesse in physiologischen Systemen geführt hat, ist das Wissen über spezifische Auswirkungen der Proteinoxidation in Lebensmitteln oder die Rolle “oxidierter” Lebensmittelproteine für den menschlichen Körper vergleichsweise gering. Oxidationsreaktionen an Lebensmittelproteinen können während des gesamten Verarbeitungsprozesses stattfinden – von der Primärproduktion bis zur Verdauung im Darm. In dem vorliegenden Aufsatz soll das derzeitige Wissen über die Mechanismen der Oxidation von Lebensmittelproteinen aus chemischer, technologischer und ernährungsphysiologischer Sicht zusammengefasst und eine Klassifizierung der einzelnen Reaktionen vorgenommen werden. Verschiedene analytische Ansätze werden verglichen, und der Zusammenhang zwischen der Oxidation von Lebensmittelproteinen und oxidativem Stress in vivo wird kritisch bewertet.

show abstract

Key role of cysteine residues and sulfenic acids in thermal- and H2O2-mediated modification of β-lactoglobulin

Cited by 34 publications

References 42 publications

The Chemistry of Protein Oxidation in Food

The Chemistry of Protein Oxidation in Food

Protein cysteine oxidation in redox signaling: Caveats on sulfenic acid detection and quantification

Die Chemie der Proteinoxidation in Lebensmitteln

Contact Info

Product

Resources

About