A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state

Autor: Kimberly Rizzolo, Steven E. Cohen, Andrew C. Weitz, Madeline M. López Muñoz, Michael P. Hendrich, Catherine L. Drennan, Sean J. Elliott
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/s41467-019-09020-4
Popis: The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods.
Databáze: Directory of Open Access Journals