Analysis of Methanobactin from Methylosinus Trichosporium OB3b by Ion Mobility Mass Spectrometry (CAT#: STEM-ST-0185-LJX)

Introduction

Methanobactins (mbs) are low molecular mass copper binding chromopeptides analogous to pyoverdin class iron-binding siderophores. Mb produced by Methylosinus trichosporium OB3b (mb-OB3b) has been used as a model molecule for methanobactin although the amino acid sequence of mb-OB3b differs significantly from other characterized mbs. In particular, there is the presence of a pair of cystine residues which are absent in other characterized mbs. The role of the Cys3–Cys6 in copper binding, Cu(II) reduction and its role on the mb-OB3b structure remains in debate. Here, we use a single-step dithiothreitol treatment as an effective method in reducing the disulfide bond allowing in-depth ion mobility-mass spectrometry (IM-MS) analysis.