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Fig. 3 | BMC Biochemistry

Fig. 3

From: Effects of protonation on the hydrolysis of triphosphate in vacuum and the implications for catalysis by nucleotide hydrolyzing enzymes

Fig. 3

Energy profiles (in kcal mol−1) for methyl triphosphate hydrolysis in different protonation states. a No protons on the triphosphate (nP = 0). b Single protonation (nP = 1). Double protonation (nP = 2) resulting in c concurrent reactions or d sequential reactions. e triple protonation (nP = 3). Greek letters (α,β,γ) indicate on which phosphate group the proton is located (see Fig. 1 for nomenclature). The energy barriers seen here correspond to those listed in Tables 1 and 2. The energy is plotted as a function of the curvilinear reaction coordinate (λ), which measure the progress of the reaction as the sum of conformational changes that occur along the MEP (in terms of RMS-change in all atomic coordinates), starting from the reactant state (λ = 0). Here λ is normalized by the total length of the curvilinear MEP, so that the hydrolysis product has λ = 1

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