6. Conclusions
With the development of laser excitation and detection systems, it has become possible to consider analyses that have otherwise been beyond the capacity of experimentalists. In this investigation, a case is made for the development of a device to analyse ATP synthase activity in-vivo. Such analyses ultimately have applications in clinical practice, particularly in the field of mitochondrial disorders, of both nuclear and mitochondrial DNA origin.
Keywords
- Noncatalytic Site
- Acrylamide Quenching
- Single Tryptophan Residue
- Modify Amino Acid Residue
- Fluorescent Resonant Energy Transfer
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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7. References
A. Baracca, S. Barogi, V. Carelli, G. Lenaz, and G. Solaini, Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase 6 gene encoding subunit a, J. Biol. Chem., 275, 4177–82 (2000).
Y. Wada, Y. Sambogni, and M. Futai, Biological nano motor, ATP synthase F0F1: from catalysis to γεc10–12 subunit assembly rotation. Biochem. Biophys. Acta, 1459, 499–505 (2000).
P. Dimroth, U. Matthey, and G. Kaim, Critical evaluation of the one-versus the two-channel model for the operation of the ATP synthase’s F0 motor. Biochem. Biophys. Acta, 1459, 506–513 (2002)
R. H. Fillingame, W. Jiang, O. Y. Dmitriev, and P. C. Jones, Structural interpretations of F(0) rotary function in the Escherichia coli F(1)F(0) ATP synthase.. Biochim. Biophys. Acta. 1458(2–3), 387–403 (2000)
J. Weber and A. E. Senior, Features of F(1)-ATPase catalytic and noncatalytic sites revealed by fluorescence lifetimes and acrylamide quenching of specifically inserted tryptophan residues. Biochemistry 39: 5287–94. (2000)
P. D. Gavin, R. J. Devenish, and M. Prescott, FRET reveals changes in the F1-stator stalk interaction during activity of F1F0-ATP synthase. Biochim. Biophys. Acta. 1607, 167–79 (2003)
H. Omote, N. Sambonmatsu, K. Sito, Y. Sambongi, A. Iwamoto-Kihara, T. Yanagida, Y. Wada, and M. Futai, The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli. Proc. Nat. Acad. Sci., USA, 96, 7780–7784 (1999)
P. D. Gavin, M. Prescott, S. E. Luff, and R. J. Devenish, Cross-linking ATP synthase complexes in vivo eliminates mitochondrial cristae. J. Cell. Sci. 117, 2333–43 (2004)
P. Turina, Structural changes during ATP hydrolysis activity of the ATP synthase from Escherichia coli as revealed by fluorescent probes. J Bioenerg. Biomembr. 32: 373–81, (2000)
M. Borsch, M. Diez, B. Zimmermann, R. Reuter, and P. Graber, Stepwise rotation of the gamma-subunit of EF(0)F(1)-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer. FEBS Lett. 527, 147–52 (2002)
M. Diez, B. Zimmermann, M. Borsch, M. Konig, E. Schweinberger, S. Steigmiller, R. Reuter, S. Felekyan, V. Kudryavtsev, C. A. Seidel, and P. Graber, Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase. Nat. Struct. Mol. Biol. 11, 135–41 (2004)
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Maguire, D., Shah, J., McCabe, M. (2006). Assaying ATP Synthase Rotor Activity. In: Cicco, G., Bruley, D.F., Ferrari, M., Harrison, D.K. (eds) Oxygen Transport to Tissue XXVII. Advances in Experimental Medicine and Biology, vol 578. Springer, Boston, MA . https://doi.org/10.1007/0-387-29540-2_11
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