ArticleThe Biochemical journal2016
Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolacea.Archives of biochemistry and biophysics · 2019Article
- Radical Trapping Study of the Relaxation ofReactive oxygen species (Apex, N.C.) · 2018Article
- Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.The Biochemical journal · 2017Article
- Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.FEBS letters · 2017Article
- LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess HChemical science · 2017Article
- A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Biochemistry · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In the absence of its substrate, the auto-reduction of the high-valent bis-Fe(IV) state of the dihaem enzyme MauG is coupled to oxidative damage of a methionine residue. Transient kinetic and solvent isotope effect studies reveal that this process occurs via two sequential long-range electron transfer (ET) reactions from methionine to the haems. The first ET is coupled to proton transfer (PT) to the haems from solvent via an ordered water network. The second ET is coupled to PT at the methionine site and occurs during the oxidation of the methionine to a sulfoxide. This process proceeds via Compound I- and Compound II-like haem intermediates. It is proposed that the methionine radical is stabilized by a two-centre three-electron (2c3e) bond. This provides insight into how oxidative damage to proteins may occur without direct contact with a reactive oxygen species, and how that damage can be propagated through the protein.
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Registered trials
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