Specific oxidation of methionine to methionine sulfoxide by dimethyl sulfoxide

1976 ◽  
Vol 24 (1) ◽  
pp. 26-31 ◽  
Author(s):  
Samuel H. Lipton ◽  
C. E. Bodwell
Keyword(s):  
Dimethyl Sulfoxide ◽  
Methionine Sulfoxide ◽  
Oxidation Of Methionine ◽  
Specific Oxidation

scholarly journals Peptide-Bound Methionine Sulfoxide (MetO) Levels and MsrB2 Abundance Are Differentially Regulated during the Desiccation Phase in Contrasted Acer Seeds

Antioxidants ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 391 ◽  
Author(s):  
Natalia Wojciechowska ◽  
Shirin Alipour ◽  
Ewelina Stolarska ◽  
Karolina Bilska ◽  
Pascal Rey ◽  
...  
Keyword(s):  
Desiccation Tolerance ◽  
Methionine Sulfoxide ◽  
Redox Status ◽  
Embryonic Axes ◽  
Seed Desiccation ◽  
Methionine Sulfoxide Reductases ◽  
Norway Maple ◽  
Orthodox Seeds ◽  
Oxidation Of Methionine ◽  
Reduced Forms

Norway maple and sycamore produce desiccation-tolerant (orthodox) and desiccation-sensitive (recalcitrant) seeds, respectively. Drying affects reduction and oxidation (redox) status in seeds. Oxidation of methionine to methionine sulfoxide (MetO) and reduction via methionine sulfoxide reductases (Msrs) have never been investigated in relation to seed desiccation tolerance. MetO levels and the abundance of Msrs were investigated in relation to levels of reactive oxygen species (ROS) such as hydrogen peroxide, superoxide anion radical and hydroxyl radical (•OH), and the levels of ascorbate and glutathione redox couples in gradually dried seeds. Peptide-bound MetO levels were positively correlated with ROS concentrations in the orthodox seeds. In particular, •OH affected MetO levels as well as the abundance of MsrB2 solely in the embryonic axes of Norway maple seeds. In this species, MsrB2 was present in oxidized and reduced forms, and the latter was favored by reduced glutathione and ascorbic acid. In contrast, sycamore seeds accumulated higher ROS levels. Additionally, MsrB2 was oxidized in sycamore throughout dehydration. In this context, the three elements •OH level, MetO content and MsrB2 abundance, linked together uniquely to Norway maple seeds, might be considered important players of the redox network associated with desiccation tolerance.

scholarly journals Oxidation of Methionine 77 in Calmodulin Alters Mouse Development and Behavior

2018 ◽  
Author(s):  
Méry Marimoutou ◽  
Danielle A. Springer ◽  
Chengyu Liu ◽  
Geumsoo Kim ◽  
Rodney Levine
Keyword(s):  
Open Field ◽  
Stress Test ◽  
Young Male ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Mutant Mice ◽  
Wild Type ◽  
Mouse Development ◽  
Oxidation Of Methionine

Methionine 77 in calmodulin can be stereospecifically oxidized to methionine sulfoxide by mammalian methionine sulfoxide reductase A. Whether this has in vivo significance is unknown. We therefore created a mutant mouse in which wild-type calmodulin-1 was replaced by a calmodulin containing a mimic of methionine sulfoxide at residue 77. Total calmodulin levels were unchanged in the homozygous M77Q mutant, which is viable and fertile. No differences were observed on learning tests, including the Morris water maze and associative learning. Cardiac stress test results were also the same for mutant and wild type mice. .However, young male and female mice were 20% smaller than wild type mice, although food intake was normal for their weight. Young M77Q mice were notably more active and exploratory than wild type mice. This behavior difference was objectively documented on the treadmill and open field tests. The mutant mice ran 20% longer on the treadmill than controls, and in the open field test, the mutant mice explored more than controls and exhibited reduced anxiety These phenotypic differences bore a similarity to those observed in mice lacking calcium/calmodulin kinase Iiα (CaMKIIα). We then showed that M77Q calmodulin was less effective in activating CaMKIIα than wild type calmodulin. Thus, characterization of the phenotype of a mouse expressing a constitutively active mimic of calmodulin led to the identification of the first calmodulin target that can be differentially regulated by the oxidation state of Met77. We conclude that reversible oxidation of methionine 77 in calmodulin by MSRA can regulate cellular function.

scholarly journals Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior

Antioxidants ◽  
2018 ◽  
Vol 7 (10) ◽  
pp. 140 ◽  
Author(s):  
Méry Marimoutou ◽  
Danielle Springer ◽  
Chengyu Liu ◽  
Geumsoo Kim ◽  
Rodney Levine
Keyword(s):  
Open Field ◽  
Stress Test ◽  
Field Tests ◽  
Young Male ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Mutant Mice ◽  
Wild Type ◽  
Oxidation Of Methionine

Methionine 77 in calmodulin can be stereospecifically oxidized to methionine sulfoxide by mammalian methionine sulfoxide reductase A. Whether this has in vivo significance is unknown. We therefore created a mutant mouse in which wild type calmodulin-1 was replaced by a calmodulin containing a mimic of methionine sulfoxide at residue 77. Total calmodulin levels were unchanged in the homozygous M77Q mutant, which is viable and fertile. No differences were observed on learning tests, including the Morris water maze and associative learning. Cardiac stress test results were also the same for mutant and wild type mice. However, young male and female mice were 20% smaller than wild type mice, although food intake was normal for their weight. Young M77Q mice were notably more active and exploratory than wild type mice. This behavior difference was objectively documented on the treadmill and open field tests. The mutant mice ran 20% longer on the treadmill than controls and in the open field test, the mutant mice explored more than controls and exhibited reduced anxiety. These phenotypic differences bore a similarity to those observed in mice lacking calcium/calmodulin kinase IIα (CaMKIIα). We then showed that MetO77 calmodulin was less effective in activating CaMKIIα than wild type calmodulin. Thus, characterization of the phenotype of a mouse expressing a constitutively active mimic of calmodulin led to the identification of the first calmodulin target that can be differentially regulated by the oxidation state of Met77. We conclude that reversible oxidation of methionine 77 in calmodulin by MSRA has the potential to regulate cellular function.

scholarly journals In Vivo Effects of Methionine Sulfoxide Reductase Deficiency in Drosophila melanogaster

Antioxidants ◽  
2018 ◽  
Vol 7 (11) ◽  
pp. 155 ◽  
Author(s):  
Lindsay Bruce ◽  
Diana Singkornrat ◽  
Kelsey Wilson ◽  
William Hausman ◽  
Kelli Robbins ◽  
...  
Keyword(s):  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Model Organisms ◽  
Methionine Sulfoxide Reductase A ◽  
Methionine Sulfoxide Reductases ◽  
Methionine Residues ◽  
Oxidation Of Methionine ◽  
And Function ◽  
In Vivo Effects

The deleterious alteration of protein structure and function due to the oxidation of methionine residues has been studied extensively in age-associated neurodegenerative disorders such as Alzheimer’s and Parkinson’s Disease. Methionine sulfoxide reductases (MSR) have three well-characterized biological functions. The most commonly studied function is the reduction of oxidized methionine residues back into functional methionine thus, often restoring biological function to proteins. Previous studies have successfully overexpressed and silenced MSR activity in numerous model organisms correlating its activity to longevity and oxidative stress. In the present study, we have characterized in vivo effects of MSR deficiency in Drosophila. Interestingly, we found no significant phenotype in animals lacking either methionine sulfoxide reductase A (MSRA) or methionine sulfoxide reductase B (MSRB). However, Drosophila lacking any known MSR activity exhibited a prolonged larval third instar development and a shortened lifespan. These data suggest an essential role of MSR in key biological processes.

Oxidation of methionine to methionine sulfoxide as a side reaction of cyanogen bromide cleavage

1982 ◽  
Vol 119 (1) ◽  
pp. 73-77 ◽  
Author(s):  
Regula Joppich-Kuhn ◽  
Jeffrey A. Corkill ◽  
Roger W. Giese
Keyword(s):  
Cyanogen Bromide ◽  
Side Reaction ◽  
Methionine Sulfoxide ◽  
Oxidation Of Methionine

Oxyhalogen–sulfur chemistry — Kinetics and mechanism of oxidation of methionine by aqueous iodine and acidified iodate

2009 ◽  
Vol 87 (6) ◽  
pp. 689-697 ◽  
Author(s):  
Edward Chikwana ◽  
Bradley Davis ◽  
Moshood K. Morakinyo ◽  
Reuben H. Simoyi
Keyword(s):  
Methionine Sulfoxide ◽  
Molecular Iodine ◽  
Reaction Scheme ◽  
Direct Reaction ◽  
Sulfur Chemistry ◽  
Reaction Characteristics ◽  
Mechanism Of Oxidation ◽  
Oxidation Of Methionine ◽  
Simple Network ◽  
Clock Reaction

The oxidation of methionine (Met) by acidic iodate and aqueous iodine was studied. Though the reaction is a simple two-electron oxidation to give methionine sulfoxide (Met–S=O), the dynamics of the reaction are, however, very complex, characterized by clock reaction characteristics and transient formation of iodine. In excess methionine conditions, the stoichiometry of the reaction was deduced to be IO3– + 3Met → I– + 3Met–S=O. In excess iodate, the iodide product reacts with iodate to give a final product of molecular iodine and a 2:5 stoichiometry: 2IO3– + 5Met + 2H+ → I2 + 5Met–S=O + H2O. The direct reaction of iodine and methionine is slow and mildly autoinhibitory, which explains the transient formation of iodine, even in conditions of excess methionine in which iodine is not a final product. The whole reaction scheme could be simulated by a simple network of 11 reactions.

scholarly journals Fibrin Clot Structure and Mechanics Associated with Specific Oxidation of Methionine Residues in Fibrinogen

2012 ◽  
Vol 103 (11) ◽  
pp. 2399-2407 ◽  
Author(s):  
Katie M. Weigandt ◽  
Nathan White ◽  
Dominic Chung ◽  
Erica Ellingson ◽  
Yi Wang ◽  
...  
Keyword(s):  
Fibrin Clot ◽  
Methionine Residues ◽  
Oxidation Of Methionine ◽  
Specific Oxidation ◽  
Clot Structure
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