Zn(ii) and Cu(i/ii) Binding to Alternative Metal Binding Peptide Using Fluorescence and Ion Mobility - Mass Spectrometry Techniques

Document Type


Degree Name

Master of Science (MS)



Date of Award

Summer 2017


Methanotrophic bacteria are the prokaryotic organisms that oxidize methane to produce a small copper chelating molecule called methanobactin (Mb) and are unique in their ability to utilize methane as sole source of energy. The methanobactins produced by Methylosinus trichosporium (mb-OB3b), currently characterized as modified chromopetides that bind to Cu(I) and other metals with high affinity, are assumed to mediate copper acquisition from the environment for particulate methane monooxygenase (pMMO) enzyme. Current research involves study of Cu(I/II) and Zn(II) binding to alternative metal binding peptide with sequence CH3CO-His 1-Cys2-Gly3-Pro4-Tyr5-His 6-Cys7-NH2 (amb5B, MW-856.99 Da) as a function of pH and Zn(II), Cu(I/II) concentration using fluorescence and ion mobility-mass spectrometry techniques. Structural importance of disulfide linkage and metal binding profile of analog methanobactin were studied. Collision-induced dissociation (CID) experiments were conducted to induce fragmentation of peptide ions in gas phase using mass spectrometry. A binding profile of the analog methanobactin with metal ions like Zn(II) and Cu(I/II) were developed in comparison to fluorescence spectroscopy.


Dr.Laurence A. Angel

Subject Categories

Chemistry | Physical Sciences and Mathematics