ArticleBiochemistry2012
Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- Heme Binding to HupZ with a C-Terminal Tag from Group A Streptococcus.Molecules (Basel, Switzerland) · 2021Article
- Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates.The Journal of biological chemistry · 2020Article
- MbnH is a diheme MauG-like protein associated with microbial copper homeostasis.The Journal of biological chemistry · 2019Article
- A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.Nature communications · 2019Article
- Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.Journal of inorganic biochemistry · 2017Article
- Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.Angewandte Chemie (International ed. in English) · 2015Article
- Bis-Fe(IV): nature's sniper for long-range oxidation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- A simple method to engineer a protein-derived redox cofactor for catalysis.Biochimica et biophysica acta · 2014Article
- Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.Biochemistry · 2014Article
- MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Archives of biochemistry and biophysics · 2014Review
- MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.Dalton transactions (Cambridge, England : 2003) · 2013Review
- Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.Annual review of biochemistry · 2013Review
- Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.FEBS letters · 2012Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
MauG is a diheme enzyme possessing a five-coordinate high-spin heme with an axial His ligand and a six-coordinate low-spin heme with His-Tyr axial ligation. A Ca(2+) ion is linked to the two hemes via hydrogen bond networks, and the enzyme activity depends on its presence. Removal of Ca(2+) altered the electron paramagnetic resonance (EPR) signals of each ferric heme such that the intensity of the high-spin heme was decreased and the low-spin heme was significantly broadened. Addition of Ca(2+) back to the sample restored the original EPR signals and enzyme activity. The molecular basis for this Ca(2+)-dependent behavior was studied by magnetic resonance and Mössbauer spectroscopy. The results show that in the Ca(2+)-depleted MauG the high-spin heme was converted to a low-spin heme and the original low-spin heme exhibited a change in the relative orientations of its two axial ligands. The properties of these two hemes are each different than those of the heme in native MauG and are now similar to each other. The EPR spectrum of Ca(2+)-free MauG appears to describe one set of low-spin ferric heme signals with a large g(max) and g anisotropy and a greatly altered spin relaxation property. Both EPR and Mössbauer spectroscopic results show that the two hemes are present as unusual highly rhombic low-spin hemes in Ca(2+)-depleted MauG, with a smaller orientation angle between the two axial ligand planes. These findings provide insight into the correlation of enzyme activity with the orientation of axial heme ligands and describe a role for the calcium ion in maintaining this structural orientation that is required for activity.
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