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Eur. J. Mass Spectrom. DOI: 10.1255/ejms.594

Mass Spectrometric Detection of Protein, Lipid, and Heme Components of Cytochrome c Oxidase from R. sphaeroides and the Stabilization of Non-covalent Complexes from the Enzyme

Anne M. Distler and John Allison
Department of Chemistry, Michigan State University, East Lansing, MI 48, USA
Carrie Hiser, Ling Qin, Yasmin Hilmi and Shelagh Ferguson-Miller
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48, USA

ABSTRACT:
The cytochrome c oxidase enzyme from the Rhodobacter sphaeroides bacteria exists as a complex of four peptide subunits, two hemes, and a variety of lipids and metal ions held together by non-covalent forces. While the native enzyme functions as an associated unit, this complex usually dissociates during MALDI-TOF analysis. Through the use of matrix additives such as sucrose, the complete complex and partial complexes can be stabilized in the MALDI-TOF experiment. The dissociation of the complex allows for the detection of the components of the enzyme. The direct detection of associated lipids from an aqueous solution of the intact enzyme may eliminate the need for enzyme disruption and lipid extraction. The partial dissociation of multisubunit enzymes in such experiments may allow for the determination of subunit-subunit and subunit-lipid interactions

Keywords: MALDI, enzyme, non-covalent complex, lipids

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