ArticleInternational journal of molecular sciences2023
Histidine-Bound Dinitrosyl Iron Complexes: Antioxidant and Antiradical Properties.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 11 citations in OpenAlex.
- Protein-bound nitrosyl iron complexes: long-lived physiological form of nitric oxide.Medical gas research · 2026Article
- Multi-omics-based metabolomic kinetics study of corn stover fermented by combined probiotic and enzymatic treatment.BMC microbiology · 2026Article
- Antioxidant Action of Dinitrosyl Iron Complexes in Model Systems Containing CytochromeMolecules (Basel, Switzerland) · 2025Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
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
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