Jump to main content
Jump to site search

Issue 1, 2017
Previous Article Next Article

Methanobactins: from genome to function

Author affiliations


Methanobactins (Mbns) are ribosomally produced, post-translationally modified peptide (RiPP) natural products that bind copper with high affinity using nitrogen-containing heterocycles and thioamide groups. In some methanotrophic bacteria, Mbns are secreted under conditions of copper starvation and then re-internalized as a copper source for the enzyme particulate methane monooxygenase (pMMO). Genome mining studies have led to the identification and classification of operons encoding the Mbn precursor peptide (MbnA) as well as a number of putative transport, regulatory, and biosynthetic proteins. These Mbn operons are present in non-methanotrophic bacteria as well, suggesting a broader role in and perhaps beyond copper acquisition. Genetic and biochemical studies indicate that specific operon-encoded proteins are involved in Mbn transport and provide insight into copper-responsive gene regulation in methanotrophs. Mbn biosynthesis is not yet understood, but combined analysis of Mbn structures, MbnA sequences, and operon content represents a powerful approach to elucidating the roles of specific biosynthetic enzymes. Future work will likely lead to the discovery of unique pathways for natural product biosynthesis and new mechanisms of microbial metal homeostasis.

Graphical abstract: Methanobactins: from genome to function

Back to tab navigation

Supplementary files

Article information

20 Sep 2016
24 Nov 2016
First published
24 Nov 2016

Metallomics, 2017,9, 7-20
Article type

Methanobactins: from genome to function

L. M. K. Dassama, G. E. Kenney and A. C. Rosenzweig, Metallomics, 2017, 9, 7
DOI: 10.1039/C6MT00208K

Social activity

Search articles by author