Spectral and thermodynamic properties of methanobactin from γ-proteobacterial methane oxidizing bacteria: A case for copper competition on a molecular level

Methanobactin (mb) is a low molecular mass copper-binding molecule analogous to iron-binding siderophores. The molecule is produced by many methanotrophic or methane oxidizing bacteria (MOB), but has only been characterized to date in one MOB, Methylosinus trichosporium OB3b. To explore the potential molecular diversity in this novel class of metal binding compound, the spectral (UV–visible, fluorescent, and electron paramagnetic resonance) and thermodynamic properties of mb from two γ-proteobacterial MOB, Methylococcus capsulatus Bath and Methylomicrobium album BG8, were determined and compared to the mb from the α-proteobacterial MOB, M. trichosporium OB3b. The mb from both γ-proteobacterial MOB differed from the mb from M. trichosporium OB3b in molecular mass and spectral properties. Compared to mb from M. trichosporium OB3b, the extracellular concentrations were low, as were copper-binding constants of mb from both γ-proteobacterial MOB. In addition, the mb from M. trichosporium OB3b removed Cu(I) from the mb of both γ-proteobacterial MOB. Taken together the results suggest mb may be a factor in regulating methanotrophic community structure in copper-limited environments.

Graphical AbstractThe properties of methanobactin (mb) from Methylococcus capsulatus Bath (Mc–mb) and Methylomicrobium album BG8 (BG8–mb) were determined and compared to mb from Methylosinus trichosporium OB3b (OB3b–mb). The higher binding constants associated with mb from M. trichosporium OB3b (OB3b–mb) and the ability of OB3b–mb to remove copper from Cu(I) containing Mc–mb (Mc–Cu–mb) and BG8–mb (BG8-Cu–mb), suggest mb may influence methanotrophic community structure.Figure optionsDownload as PowerPoint slide