New dinitrosyl iron complexes bound with physiologically active dipeptide carnosine

Шумаев, К. Б.; Kosmachevskaya, O. V.; Nasybullina, E. I.; Gromov, S.; Novikov, A A; Топунов, А. Ф.

doi:10.1007/s00775-016-1418-z

Cited by 10 publications

(10 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…As for HNO, there is currently little evidence that it plays a significant physiological role [37]. However due to the non-innocent nature of NO as a ligand [38–40], it is difficult to determine the exact oxidation state of the central iron, or the NO in DNICs, such that it is possible that DNICs themselves could act as nitroxyl donors if the NO in the DNICs is in the NO - form, as proposed by some investigators [41–43]. This would make it harder to differentiate whether DNICs are releasing NO in FeCN due to the oxidation of the Fe 2+ center, or due to the oxidation of a nitroxyl intermediate, or the direct oxidation of an iron-bound nitroxyl moiety.…”

Section: Discussionmentioning

confidence: 99%

Detection of dinitrosyl iron complexes by ozone-based chemiluminescence

et al. 2018

View full text Add to dashboard Cite

Dinitrosyl iron complexes (DNICs) are important intermediates in the metabolism of nitric oxide (NO). They have been considered to be NO storage adducts able to release NO, scavengers of excess NO during inflammatory hypotensive shock, and mediators of apoptosis in cancer cells, among many other functions. Currently, all studies of DNICs in biological matrices use electron paramagnetic resonance (EPR) for both detection and quantification. EPR is limited, however, by its ability to detect only paramagnetic mononuclear DNICs even though EPR-silent binuclear are likely to be prevalent. Furthermore, physiological concentrations of mononuclear DNICs are usually lower than the EPR detection limit (1 μM). We have thus developed a chemiluminescence-based method for the selective detection of both DNIC forms at physiological, pathophysiological, and pharmacologic conditions. We have also demonstrated the use of the new method in detecting DNIC formation in the presence of nitrite and nitrosothiols within biological fluids and tissue. This new method, which can be used alone or in tandem with EPR, has the potential to offer insight about the involvement of DNICs in many NO-dependent pathways.

show abstract

Section: Discussionmentioning

confidence: 99%

Detection of dinitrosyl iron complexes by ozone-based chemiluminescence

et al. 2018

View full text Add to dashboard Cite

show abstract

“…The class of NO-donor carnosine derivatives also includes DNICs associated with carnosine. We have previously shown that carnosine in the presence of the nitroxyl anion (NO − ) and iron ions participates in DNIC formation [16]. In that work, Angeli's salt (sodium trioxidinitrate) was the donor of HNO (the protonated form of the nitroxyl anion) (Figure 1).…”

Section: Introductionmentioning

confidence: 88%

“…The iron in DNICs can also be coordinated with phosphate anions, with the nitrogen of the histidine imidazole ring, and with some other ligands [3,11,15,16]. DNICs, whose ligands are histidine residues in peptides and proteins (Figure 1), have received the most attention.…”

Section: Introductionmentioning

confidence: 99%

Histidine-Bound Dinitrosyl Iron Complexes: Antioxidant and Antiradical Properties

Shumaev,

Kosmachevskaya,

Nasybullina

et al. 2023

IJMS

Self Cite

View full text Add to dashboard Cite

Dinitrosyl iron complexes (DNICs) are important physiological derivatives of nitric oxide. These complexes have a wide range of biological activities, with antioxidant and antiradical ones being of particular interest and importance. We studied the interaction between DNICs associated with the dipeptide L-carnosine or serum albumin and prooxidants under conditions mimicking oxidative stress. The ligands of these DNICs were histidine residues of carnosine or His39 and Cys34 in bovine serum albumin. Carnosine-bound DNICs reduced the level of piperazine free radicals in the reaction system containing tert-butyl hydroperoxide (t-BOOH), bivalent iron ions, a nitroxyl anion donor (Angeli’s salt), and HEPES buffer. The ability of carnosine DNICs to intercept organic free radicals produced from t-BOOH decay could lead to this effect. In addition, carnosine DNICs reacted with the superoxide anion radical (O2•−) formed in the xanthine/xanthine oxidase enzymatic system. They also reduced the oxoferryl form of the heme group formed in the reaction of myoglobin with t-BOOH. DNICs associated with serum albumin were found to be rapidly destroyed in a model system containing metmyoglobin and t-BOOH. At the same time, these protein DNICs inhibited the t-BOOH-induced oxidative degradation of coenzymes Q9 and Q10 in rat myocardial homogenate. The possible mechanisms of the antioxidant and antiradical action of the DNICs studied and their role in the metabolism of reactive oxygen and nitrogen species are discussed.

show abstract

“…We have previously shown, that physiological metabolites of NO-dinitrosyl iron complexes (DNICs) can protect both: Hb against peroxide-caused oxidative stress [196,197] and RBCs against hemolysis induced with hypochlorous acid [198]. Taking into account that we have obtained DNICs containing carnosine as a ligand [199], it is possible to suggest that carnosine DNICs can protect RBCs under carbonyl stress, by combining the protective properties of both components.…”

Section: Pharmacological Interventions and Future Perspectivesmentioning

confidence: 95%

Carbonyl Stress in Red Blood Cells and Hemoglobin

2021

Self Cite

View full text Add to dashboard Cite

The paper overviews the peculiarities of carbonyl stress in nucleus-free mammal red blood cells (RBCs). Some functional features of RBCs make them exceptionally susceptible to reactive carbonyl compounds (RCC) from both blood plasma and the intracellular environment. In the first case, these compounds arise from the increased concentrations of glucose or ketone bodies in blood plasma, and in the second—from a misbalance in the glycolysis regulation. RBCs are normally exposed to RCC—methylglyoxal (MG), triglycerides—in blood plasma of diabetes patients. MG modifies lipoproteins and membrane proteins of RBCs and endothelial cells both on its own and with reactive oxygen species (ROS). Together, these phenomena may lead to arterial hypertension, atherosclerosis, hemolytic anemia, vascular occlusion, local ischemia, and hypercoagulation phenotype formation. ROS, reactive nitrogen species (RNS), and RCC might also damage hemoglobin (Hb), the most common protein in the RBC cytoplasm. It was Hb with which non-enzymatic glycation was first shown in living systems under physiological conditions. Glycated HbA1c is used as a very reliable and useful diagnostic marker. Studying the impacts of MG, ROS, and RNS on the physiological state of RBCs and Hb is of undisputed importance for basic and applied science.

show abstract

New dinitrosyl iron complexes bound with physiologically active dipeptide carnosine

Cited by 10 publications

References 69 publications

Detection of dinitrosyl iron complexes by ozone-based chemiluminescence

Detection of dinitrosyl iron complexes by ozone-based chemiluminescence

Histidine-Bound Dinitrosyl Iron Complexes: Antioxidant and Antiradical Properties

Carbonyl Stress in Red Blood Cells and Hemoglobin

Contact Info

Product

Resources

About