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

Kimberly Rizzolo; Steven E. Cohen; Andrew C. Weitz; Madeline M. López Muñoz; Michael P. Hendrich; Catherine L. Drennan; Sean J. Elliott

doi:10.1038/s41467-019-09020-4

Nature Communications (Mar 2019)

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

Kimberly Rizzolo,
Steven E. Cohen,
Andrew C. Weitz,
Madeline M. López Muñoz,
Michael P. Hendrich,
Catherine L. Drennan,
Sean J. Elliott

Affiliations

Kimberly Rizzolo: Boston University, Department of Chemistry
Steven E. Cohen: Massachusetts Institute of Technology, Department of Chemistry
Andrew C. Weitz: Carnegie Mellon University, Department of Chemistry
Madeline M. López Muñoz: Boston University, Department of Chemistry
Michael P. Hendrich: Carnegie Mellon University, Department of Chemistry
Catherine L. Drennan: Massachusetts Institute of Technology, Department of Chemistry
Sean J. Elliott: Boston University, Department of Chemistry

DOI: https://doi.org/10.1038/s41467-019-09020-4
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 10

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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