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Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-Fe(IV) state of MauG
The high-valent state of the diheme enzyme MauG exhibits charge–resonance (CR) stabilization in which the major species is a bis-Fe(IV) state with one heme present as Fe(IV)=O and the other as Fe(IV) with axial heme ligands provided by His and Tyr side chains. In the absence of its substrate, the hi...
Sparad:
| I publikationen: | Proc Natl Acad Sci U S A |
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| Huvudupphovsmän: | , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
National Academy of Sciences
2015
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4568243/ https://ncbi.nlm.nih.gov/pubmed/26283395 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1510986112 |
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