Browse by author
Lookup NU author(s): Professor David Graham
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Siderophores are extracellular iron-binding compounds that mediate iron transport into many cells. We present evidence of analogous molecules for copper transport from methane-oxidizing bacteria, represented here by a small fluorescent chromopeptide (C45N12O14H62Cu; 1216 Da) produced by Methylosinus trichosporium OB3b. The crystal structure of this compound, methanobactin, was resolved to 1.15 Å. It is comprised of a tetrapeptide, a tripeptide, and several unique moieties, including two 4-thionyl-5-hydroxy-imidazole chromophores that coordinate the copper, a pyrrolidine that confers a bend in the overall chain, and a N-terminal isopropylester group. The copper coordination environment includes a dual N,S-donating system derived from the thionyl imidazolate moieties. Structural elucidation of this molecule has broad implications in terms of organo-copper chemistry, biological methane oxidation, and global carbon cycling.
Author(s): Kim HJ, Graham DW, DiSpirito AA, Alterman MA, Galeva N, Larive CK, Asunskis D, Sherwood PMA
Publication type: Article
Publication status: Published
Print publication date: 10/09/2004
ISSN (print): 0036-8075
ISSN (electronic): 1095-9203
Publisher: American Association for the Advancement of Science
Altmetrics provided by Altmetric