Lookup NU author(s): Professor Christopher Dennison
This is the authors' accepted manuscript of a review published in its final definitive form in 2019. For re-use rights please refer to the publishers terms and conditions.
Methanotrophs are remarkable bacteria that utilise large quantities of copper (Cu) to oxidize the potent greenhouse gas methane. To help provide the Cu they require for this process some methanotrophs can secrete the Cu-sequestering modified peptide methanobactin. These small molecules bind Cu(I) with very high affinity and crystal structures have provided insight into why this is the case, and also how the metal ion may be released within the cell. A much greater proportion of methanotrophs possess a member of a newly discovered bacterial family of copper storage proteins (the Csps). These are tetramers of four-helix bundles whose cores are lined with Cys residues enabling the binding of large numbers of Cu(I) ions. In methanotrophs, a Csp exported from the cytosol stores Cu(I) for the active site of the ubiquitous enzyme that catalyses the oxidation of methane. The presence of cytosolic Csps, not only in methanotrophs but in a wide range of bacteria, challenges the dogma that these organisms have no requirement for Cu in this location. The properties of the Csps, with an emphasis on Cu(I) binding and the structures of the sites formed, are the main focus of this review.
Author(s): Dennison C
Publication type: Review
Publication status: Published
Journal: Chemistry - A European Journal
Print publication date: 02/01/2019
Online publication date: 03/10/2018
Acceptance date: 26/09/2018
ISSN (print): 0947-6539
ISSN (electronic): 1521-3765