ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2014
Kinetics of serotonin oxidation by heme-Aβ relevant to Alzheimer's disease.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 33 citations in OpenAlex.
- The Neural Palette of Heme: Altered Heme Homeostasis Underlies Defective Neurotransmission, Increased Oxidative Stress, and Disease Pathogenesis.Antioxidants (Basel, Switzerland) · 2024Review
- Anaerobic heme recycling by gut microbes: Important methods for monitoring porphyrin production.Methods in enzymology · 2024Article
- Transition metal ions and neurotransmitters: coordination chemistry and implications for neurodegeneration.RSC chemical biology · 2023Review
- Review
- Spin state dependent peroxidase activity of heme bound amyloid β peptides relevant to Alzheimer's disease.Chemical science · 2022Article
- Relationships between Mitochondrial Dysfunction and Neurotransmission Failure in Alzheimer's Disease.Aging and disease · 2020Review
- Formation of compound I in heme bound Aβ-peptides relevant to Alzheimer's disease.Chemical science · 2019Article
- A catalytic antioxidant for limiting amyloid-beta peptide aggregation and reactive oxygen species generation.Chemical science · 2019Article
- Amyloid β and free heme: bloody new insights into the pathogenesis of Alzheimer's disease.Neural regeneration research · 2018Review
- Cytochrome c peroxidase activity of heme bound amyloid β peptides.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Interaction of apoNeuroglobin with heme-Aβ complexes relevant to Alzheimer's disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Serotonin (5-HT) is an essential neurotransmitter for cognitive functions and formation of new memories. A deficit in 5-HT dependent neuronal activity is somewhat specific for Alzheimer's disease. Metal-mediated oxidative degradation of neurotransmitters by Aβ bound to metals has been investigated. Heme-bound Aβ is found to catalyze the oxidative degradation of 5-HT leading to the formation of neurotoxic products dihydroxybitryptamine and tyrptamine-4,5-dione. The catalytic degradation of 5-HT is of first order with respect to both heme-Aβ and H2O2, and the maximum rate of 5-HT oxidation is obtained at physiological pH (pH 7-7.5). pH perturbation of the binding affinity of heme-Aβ complex for 5-HT indicates that the binding of the substrate (5-HT) is not the rate-determining step. Arg5 acts as a second-sphere residue facilitating the O-O bond cleavage, the mutation of which leads to a decrease in the rate of 5-HT oxidation. The pull effect of the Arg5 residue tends to facilitate the generation of the active oxidant, Compound I, below neutral pH, while the ionization of the phenol group of the substrate facilitates the generation of the active substrate above neutral pH. A combination of these two opposing effects results in the highest activity at physiological pH. Apart from the Arg5 residue, the Tyr10 residue is found to play a vital role in the 5-HT oxidation by heme-Aβ complexes.
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