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Manganese and copper binding properties of Mnx studied by surface induced dissociation and native mass spectrometry

ABSTRACT: The metal binding properties of Mnx (Bacillus sp.), a manganese biomineralization enzyme complex, E/F/G subunits was studied using native mass spectrometry coupled to surface induced dissociation and ion mobility. The complex consists of one MnxG subunit, and a Mnx(E3F3) heterohexamer ring. Copper ejection on MnxF subunit was observed with increased Mn titrations. Cu titrations show increased Cu adducts to all subunits. Statistically significant changes in drift time were observed for all subunits with increased Mn titrations, and fewer changes in drift time were observed for Cu titrations. Mn titrations with an inactive mutant of Mnx, Mnx H340A, showed binding of Mn to all subunits, particularly when ammonium acetate concentrations were reduced to 20 mM.

INSTRUMENT(S): SYNAPT G2-Si

ORGANISM(S): Bacillus Sp. Pl-12 (ncbitaxon:161537)

SUBMITTER: Mowei Zhou

PROVIDER: MSV000092552 | MassIVE | Fri Jul 28 17:19:00 BST 2023

REPOSITORIES: MassIVE

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