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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...

Täydet tiedot

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Bibliografiset tiedot
Julkaisussa:Biochem J
Päätekijät: Dow, Brian A., Davidson, Victor L.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2015
Aiheet:
Linkit: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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