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. 2022 Aug 23;13:965620. doi: 10.3389/fmicb.2022.965620

Figure 3.

Figure 3

Sequential conformational changes of vanadyl-nucleotides bound to specific F1-ATPase catalytic sites demonstrate the F1 binding-change mechanism. (A) Equatorial ligands determine 51V-hyperfine Parameters of VO2+. EPR spectra of VO2+ with water (top) or hydroxyl groups (bottom) as equatorial ligands. The parallel transitions (−7/2||, −5/2||, +3/2||, +5/2||, and + 7/2||) that are not superimposed with perpendicular transitions are identified. Inset: dependence of the −5/2|| transition on the type of equatorial ligands. (B) The −5/2|| transition(s) of VO2+ bound to SoF1 as: (a) VO2+–ATP at latent Site-2, (b) VO2+–ADP bound to latent Site-3, (c) VO2+–ADP bound to activated Site-3, (d) VO2+–ATP bound to activated site 3; and (e) VO2+–ATP bound to Site 1 using SoF1–ε. This figure was modified from Frasch (2000a,b) with permission of the publisher.