https://zenodo.org/record/1258619/files/article.pdf

Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences

Lipids of mitochondria

Highly reactive oxygen species that are formed during normal metabolism and under conditions of oxidative stress are able to oxidize proteins or convert lipid and carbohydrate derivatives to compounds that react with functional groups on proteins. Among other changes, these ROS-mediated reactions lead to the formation of protein carbonyl derivatives, which serves as a marker of ROS-mediated protein damage. On the basis of this marker, it is established that oxidatively damaged protein is associated with aging and some diseases. The accumulation of oxidatively damaged protein reflects the balance among a myriad of factors that govern the rates of ROS generation and the rate at which damaged protein is degraded. Peroxynitrite, which is formed under normal physiological conditions, is able to oxidize methionine residues in proteins and to nitrate tyrosine residues; however, its ability to do so is dependent on the availability of CO2, which stimulates the nitration of tyrosine residues but inhibits the oxidation of methionine residues. Nitration of tyrosine residues may contribute to peroxynitrite toxicity, as nitration precludes the phosphorylation or nucleotidylation of tyrosine residues and thereby seriously compromises one of the most important mechanisms of cellular regulation and signal transduction.

Reactive oxygen-mediated protein oxidation in aging and disease.

Towards the physiological function of uric acid

Article de synthese sur le role antimicrobien du dioxyde de carbone au niveau des aliments (eau, lait, poisson, fruits, legumes), et sur la croissance microbienne au cours de divers procedes de fermentation

The inhibition by CO2 of the growth and metabolism of micro-organisms

Different water purity provokes a great variation of the stability of ascorbic acid and isoascorbic acid solutions. The effect of temperature on ascorbate aerobic oxidation was assessed by means of Arrhenius plots from which thermodynamic parameters were derived. The presence of bovine serum albumin drastically reduces the vitamin oxidation rate regardless of stereoisomerism. On the other hand the interaction with alkaline phosphatase, an enzyme inhibited by preincubation with vitamin C, does not modify significantly the stability in the experimental conditions used.

Ascorbic acid stability in aqueous solutions.

Alkaline phosphatase inactivation by mixed function oxidation systems

The lipid composition of S. cerevisiae cells was studied in different conditions of pH and of HCO3- and CO2 concentration.

A Castelli

Papers

Ascorbic acid stability in aqueous solutions.

Alkaline phosphatase inactivation by mixed function oxidation systems

Effect of pH and CO2 concentration changes on lipids and fatty acids of Saccharomyces cerevisiae.

Specificity of lipids and coenzyme Q in mitochondrial NADH and succin-oxidase of beef heart and S. cerevisiae.

Studies on the lipids of S. cerevisiae during the growth phases.