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Converting the bis-Fe(IV) state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer
The electron transfer (ET) properties of two types of high-valent hemes were studied within the same protein matrix; the bis-Fe(IV) state of MauG and the Compound I state of Y294H MauG. The latter is formed as a consequence of mutation of the Tyr which forms the distal axial ligand of the six-coordi...
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| Published in: | Biochem J |
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| Main Authors: | , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
2015
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4860820/ https://ncbi.nlm.nih.gov/pubmed/26494530 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20150998 |
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