Insight into Metal Removal from Peptides that Sequester Copper for Methane Oxidation. Issue 18 (5th March 2018)

• Record Type: Journal Article
• Authors: Baslé, Arnaud; El Ghazouani, Abdelnasser; Lee, Jaeick; Dennison, Christopher
• Is Part Of: Chemistry. Volume 24:Issue 18(2018)
• Page Start: 4515
• Page End: 4518
• Publication Date: 2018-03-05
• Subjects: bioinorganic chemistry -- copper -- methane -- methanotrophs -- oxidation; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201706035
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: Methanobactins (Mbns) are modified peptides that sequester copper (Cu) methanotrophs use to oxidize methane. Limited structural information is available for this class of natural products, as is an understanding of how cells are able to utilize Mbn‐bound Cu. The crystal structure of Methylosinus sporium NR3K Cu I –Mbn provides further information about the structural diversity of Mbns and the first insight into their Cu‐release mechanism. Nitrogen ligands from oxazolone and pyrazinediol rings chelate Cu I along with adjacent coordinating sulfurs from thioamides. In vitro solution data are consistent with a Cu I –Mbn monomer as found for previously characterized Mbns. In the crystal structure, the N‐terminal region has undergone a conformational change allowing the formation of a Cu I 2 –Mbn2 dimer with Cu I sites bound by chelating units from adjacent chains. Such a structural alteration will facilitate Cu I release from Mbns. Abstract : Methanobactins are secreted by methanotrophs to sequester copper for methane oxidation, and bind copper with high affinity. In its crystal structure, a new methanobactin adopts a conformation that provides the first insight into how copper removal occurs from these rare examples of copper‐binding natural products.