1. Disruption of flavin homeostasis in isolated rat liver mitochondria
- Author
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N.L. Vekshin, M.S. Frolova, and Victor V. Marchenkov
- Subjects
Niacinamide ,0301 basic medicine ,Luminescence ,Dinitrocresols ,Flavin Mononucleotide ,Iron ,Riboflavin ,Biophysics ,Flavoprotein ,Mitochondria, Liver ,Flavin group ,Biochemistry ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Superoxides ,Enzymatic hydrolysis ,medicine ,Animals ,Homeostasis ,Rats, Wistar ,Molecular Biology ,Ions ,biology ,Nicotinamide ,Adenine Nucleotides ,Superoxide ,Hydrolysis ,Cell Biology ,Adenosine ,Guanine Nucleotides ,Rats ,030104 developmental biology ,chemistry ,030220 oncology & carcinogenesis ,Flavin-Adenine Dinucleotide ,biology.protein ,NAD+ kinase ,medicine.drug - Abstract
It has been shown that spontaneous release of non-covalent flavins (from flavoenzymes) begins after isolation of mitochondria from rat liver, which is hydrolyzed to riboflavin. This process is stopped by 1 mM EDTA in the incubation medium. In the presence of NADH, deflavinization of flavoproteins leads to formation of superoxide by at least of three processes. The first of these occurs in complex I as a result of the spontaneous release of FMN from the active center. This process is inhibited by adenosine and guanosine phosphates, as well as NAD, but amplified by nicotinamide. The second process is associated with enzymatic hydrolysis of FAD and FMN to riboflavin; it is blocked by EDTA, AMP, NA, NAD. The third process is associated with non-enzymatic hydrolysis of FAD by iron ions in matrix; it is blocked by EDTA and AMP.
- Published
- 2019
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