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. 2019 Mar 8;24(5):958. doi: 10.3390/molecules24050958

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Nucleotide binding in the (A) aggregated and (B) free H⁺-ATPase hexamer. The intrinsic fluorescence intensity (Figure 8) of the H⁺-ATPase at a wavelength (λ) of 332 nm in the presence of (●) ADP and (○) AMP-PCP was fitted to Equation (2) by nonlinear regression; the Hill number (n) and dissociation constants (K_d) were calculated: (A) n = 1.13 ± 0.02 and 1.20 ± 0.03; K_d = 136.0 ± 7.8 and 73.3 ± 5.8 μM for ADP and AMP-PCP, respectively; (B) n = 1.06 ± 0.02 and 1.16 ± 0.04; K_d = 190.5 ± 13.9 and 105.8 ± 12.6 μM for ADP and AMP-PCP, respectively. Insets, Hill plots for nucleotide binding, the slope (n) value of the straight lines formed was calculated by linear regression: (A) n = 1.12 ± 0.01 and 1.18 ± 0.02 for ADP and AMP-PCP, respectively; (B) n = 1.07 ± 0.01 and 1.16 ± 0.01 for ADP and AMP-PCP, respectively. Fluorescence data are the mean ± SD of three experiments.