Figure 3: Native mass spectrometry analysis of Cphy1178. | Scientific Reports

Figure 3: Native mass spectrometry analysis of Cphy1178.

From: Insight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans

Figure 3

(A) Ion-mobility MS analysis of recombinant Cphy1178 displays a charge state distribution consistent with the +26 to +29 ions of a tetrameric assembly of Cphy1178 (Top, 191.3 KDa). Ion-mobility data, displayed as a greyscale heat map (bottom) reveals that each charge states exhibit a single drift time. When corrected for charge, the drift times of all charge states are all consistent with a collision cross section of 11,000 Å2 (hashed red line). (A , Insert) A topological cartoon of the Cphy1178 tetramer using ball-and-stick representations (ball, monomer; stick, interface). Interface areas in Å2 (black) and number of salt bridges (red) are marked; and calculated collision cross section (Ω) in Å2 is given. (B) Gas phase dissociation of the Cphy1178 using collision induced dissociation leads exclusively to the appearance of monomeric Cphy1178; a 1 KDa adduct is also observed (*) (C) Partial disruption of the Cphy1178 assembly by solution-phase dissociation prior to MS analysis (using 40% v/v MeOH) leads to the appearance of both monomeric and dimeric subcomplexes.

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