Heme electron transfer in peroxidases: the propionate e-pathway.
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Summary
By selectively turning on/off different quantum regions, a new mechanism which directly involves the porphyrin ring and the heme propionates is obtained, which is named "the propionate e-pathway".
- Type
- article
- Published
- 2008-09-25
- Cited by
- 27
- References
- 1
- OpenAlex
- https://openalex.org/W1966388445
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:3390172
Keywords
Heme, Chemistry, Electron transfer, Propionate, Peroxidase
References
Cited by
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- Substituent effects of iron porphyrins: Structural, kinetic, and theoretical studies
- Peroxidase activity stabilization of cytochrome P450(BM3) by rational analysis of intramolecular electron transfer.
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- Crystallographic, Kinetic, and Spectroscopic Study of the First Ligninolytic Peroxidase Presenting a Catalytic Tyrosine*
- EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level.
- Electronic structures of heme a of cytochrome c oxidase in the redox states—Charge density migration to the propionate groups of heme a
- Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: a novel peroxidase activation mechanism.
- Nitric oxide synthase stabilizes the tetrahydrobiopterin cofactor radical by controlling its protonation state.
- Density Functional Theory Insights into the Role of the Methionine-Tyrosine-Tryptophan Adduct Radical in the KatG Catalase Reaction: O2 Release from the Oxyheme Intermediate.
- Going with the Electron Flow: Heme Electronic Structure and Electron Transfer in Cytochrome c
- Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases.
- Replacement of oxidizable residues predicted by QM-MM simulation of a fungal laccase generates variants with higher operational stability.
- Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins
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