ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2007
Redox reactivity of the heme Fe3+/Fe 2+ couple in native myoglobins and mutants with peroxidase-like activity.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 30 citations in OpenAlex.
- Redox implications of oxygen binding in hemoglobin and myoglobin: Thermodynamics of the (FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy.The FEBS journal · 2022Article
- X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.The Journal of biological chemistry · 2020Article
- Stereoselective Cyclopropanation of Electron-Deficient Olefins with a Cofactor Redesigned Carbene Transferase Featuring Radical Reactivity.ACS catalysis · 2019Article
- Extending the Nonbonded Cationic Dummy Model to Account for Ion-Induced Dipole Interactions.The journal of physical chemistry letters · 2017Article
- Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Biochimica et biophysica acta · 2016Review
- A redox signalling globin is essential for reproduction in Caenorhabditis elegans.Nature communications · 2015Article
- Intramolecular C(sp(3))H amination of arylsulfonyl azides with engineered and artificial myoglobin-based catalysts.Bioorganic & medicinal chemistry · 2014Article
- Tyrosyl radicals in dehaloperoxidase: how nature deals with evolving an oxygen-binding globin to a biologically relevant peroxidase.The Journal of biological chemistry · 2013Article
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7 authors at 2 institutions in 1 country.
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Abstract
The reaction enthalpy and entropy for the one-electron reduction of the ferric heme in horse heart and sperm whale aquometmyoglobins (Mb) have been determined exploiting a spectroelectrochemical approach. Also investigated were the T67R, T67K, T67R/S92D and T67R/S92D Mb-H variants (the latter containing a protoheme-L: -histidine methyl ester) of sperm whale Mb, which feature peroxidase-like activity. The reduction potential (E degrees ') in all species consists of an enthalpic term which disfavors Fe(3+) reduction and a larger entropic contribution which instead selectively stabilizes the reduced form. This behavior differs from that of the heme redox enzymes and electron transport proteins investigated so far. The reduction thermodynamics in the series of sperm whale Mb variants show an almost perfect enthalpy-entropy compensation, indicating that the mutation-induced changes in DeltaH(o')(rc) and DeltaS(o')(rc) are dominated by reduction-induced solvent reorganization effects. The modest changes in E degrees ' originate from the enthalpic effects of the electrostatic interactions of the heme with the engineered charged residues. The small influence that the mutations exert on the reduction potential of myoglobin suggests that the increased peroxidase activity of the variants is not related to changes in the redox reactivity of the heme iron, but are likely related to a more favored substrate orientation within the distal heme cavity.
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