Log in to save to my catalogue

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

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

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_43e89e2788134c44bc04e90574efd768

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

About this item

Full title

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

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-03, Vol.10 (1), p.1101-1101, Article 1101

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H
2
O
2
) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we present the discovery of a unique diheme peroxidase BthA conserved in all
Burkho...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_43e89e2788134c44bc04e90574efd768

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_43e89e2788134c44bc04e90574efd768

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-09020-4

How to access this item