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Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away
The diheme enzyme MauG catalyzes oxidative posttranslational modifications of a protein substrate, preMADH, that binds to the surface of MauG. The high-spin heme iron of MauG is located 40 Å from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases...
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| Veröffentlicht in: | FEBS Lett |
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| Hauptverfasser: | , , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
2017
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5905328/ https://ncbi.nlm.nih.gov/pubmed/28485817 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/1873-3468.12666 |
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