The DOI matches its Crossref record; 101 of the 103 references it cites were found in a registry or an index.
The mechanism of rotating proton pumping ATPases
Open accessAbstract
Two proton pumps, the F-ATPase (ATP synthase, FoF1) and the V-ATPase (endomembrane proton pump), have different physiological functions, but are similar in subunit structure and mechanism. They are composed of a membrane extrinsic (F1 or V1) and a membrane intrinsic (Fo or Vo) sector, and couple catalysis of ATP synthesis or hydrolysis to proton transport by a rotational mechanism. The mechanism of rotation has been extensively studied by kinetic, thermodynamic and physiological approaches. Techniques for observing subunit rotation have been developed. Observations of micron-length actin filaments, or polystyrene or gold beads attached to rotor subunits have been highly informative of the rotational behavior of ATP hydrolysis-driven rotation. Single molecule FRET experiments between fluorescent probes attached to rotor and stator subunits have been used effectively in monitoring proton motive force-driven rotation in the ATP synthesis reaction. By using small gold beads with diameters of 40-60 nm, the E. coli F1 sector was found to rotate at surprisingly high speeds (>400 rps). This experimental system was used to assess the kinetics and thermodynamics of mutant enzymes. The results revealed that the enzymatic reaction steps and the timing of the domain interactions among the beta subunits, or between the beta and gamma subunits, are coordinated in a manner that lowers the activation energy for all steps and avoids deep energy wells through the rotationally-coupled steady-state reaction. In this review, we focus on the mechanism of steady-state F1-ATPase rotation, which maximizes the coupling efficiency between catalysis and rotation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Synaptic vesicles are acidified by vacuolar H+-dependent adenosine triphosphatases (V-ATPases) that pump protons into the vesicle lumen.17”
From Synaptic and circuit functions of multitransmitter neurons in the mammalian brain (2023) · cites this paper as [17]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
Abrahams, J., Leslie, A. G., Lutter, R., & Walker, J. (1994) · Nature · doi:10.1038/370621a0 · Cited by 2,961
Direct observation of the rotation of F1-ATPase
Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (1997) · Nature · doi:10.1038/386299a0 · Cited by 2,216
THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE
Boyer, P. D. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.717 · Cited by 2,014
Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
Forgac, M. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2272 · Cited by 1,626
Molecular Architecture of the Rotary Motor in ATP Synthase
Stock, D., Leslie, A. G. W., & Walker, J. E. (1999) · Science · doi:10.1126/science.286.5445.1700 · Cited by 1,271
The vacuolar (H+)-ATPases — nature's most versatile proton pumps
Nishi, T., & Forgac, M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm729 · Cited by 1,197
Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
Yasuda, R., Noji, H., Yoshida, M., Kinosita, K., & Itoh, H. (2001) · Nature · doi:10.1038/35073513 · Cited by 819
F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° Steps
Yasuda, R., Noji, H., Kinosita, K., & Yoshida, M. (1998) · Cell · doi:10.1016/s0092-8674(00)81456-7 · Cited by 798
The V-type H+ ATPase: molecular structure and function, physiological roles and regulation
Beyenbach, K., & Wieczorek, H. (2006) · Journal of Experimental Biology · doi:10.1242/jeb.02014 · Cited by 637
Linkies, A., Graeber, K., Knight, C. A., & Leubner‐Metzger, G. (2010) · New Phytologist · doi:10.1111/j.1469-8137.2010.03249.x · Cited by 609
Mechanically driven ATP synthesis by F1-ATPase
Itoh, H., Takahashi, A., Adachi, K., Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (2004) · Nature · doi:10.1038/nature02212 · Cited by 545
The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function
Marshansky, V. N., & Futai, M. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.015 · Cited by 507
Self-citationIntersubunit rotation in active F-ATPase
Sabbert, D., Engelbrecht, S., & Junge, W. (1996) · Nature · doi:10.1038/381623a0 · Cited by 483
Proton-powered turbine of a plant motor
Seelert, H., Poetsch, A., Dencher, N. A., Engel, A. H., Stahlberg, H., & Müller, D. J. (2000) · Nature · doi:10.1038/35013148 · Cited by 465
Rotation of subunits during catalysis by Escherichia coli F1-ATPase.
Duncan, T. M., Bulygin, V. V., Zhou, Y. C., Hutcheon, M. L., & Cross, R. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.24.10964 · Cited by 461
Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F 0 F 1 ): Direct Observation
Sambongi, Y., Iko, Y., Tanabe, M., Omote, H., Iwamoto-Kihara, A., Ueda, I., Yanagida, T., Wada, Y., & Futai, M. (1999) · Science · doi:10.1126/science.286.5445.1722 · Cited by 445
Self-citationStructure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites
Menz, R. I., Walker, J. E., & Leslie, A. G. W. (2001) · Cell · doi:10.1016/s0092-8674(01)00452-4 · Cited by 439
The molecular mechanism of ATP synthesis by F1F0-ATP synthase
Senior, A. E., Nadanaciva, S., & Weber, J. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00185-8 · Cited by 408
Coupling of Rotation and Catalysis in F1-ATPase Revealed by Single-Molecule Imaging and Manipulation
Adachi, K., Oiwa, K., Nishizaka, T., Furuike, S., Noji, H., Itoh, H., Yoshida, M., & Kinosita, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.020 · Cited by 400
Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase
Diez, M., Zimmermann, B., Börsch, M., König, M., Schweinberger, E., Steigmiller, S., Reuter, R., Felekyan, S., Kudryavtsev, V., Seidel, C. A. M., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb718 · Cited by 391
Catalytic mechanism of F1-ATPase
Weber, J., & Senior, A. E. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(96)00121-1 · Cited by 376
Structure of the Rotor Ring of F-Type Na + -ATPase from Ilyobacter tartaricus
Meier, T. W., Polzer, P., Diederichs, K., Welte, W., & Dimroth, P. (2005) · Science · doi:10.1126/science.1111199 · Cited by 370
Torque generation and elastic power transmission in the rotary FOF1-ATPase
Junge, W., Sielaff, H., & Engelbrecht, S. (2009) · Nature · doi:10.1038/nature08145 · Cited by 358
Highly coupled ATP synthesis by F1-ATPase single molecules
Rondelez, Y., Tresset, G., Nakashima, T., Kato‐Yamada, Y., Fujita, H., Takeuchi, S., & Noji, H. (2005) · Nature · doi:10.1038/nature03277 · Cited by 333
Essentials for ATP Synthesis by F1F0 ATP Synthases
von Ballmoos, C., Wiedenmann, A., & Dimroth, P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.104803 · Cited by 332
The rotary mechanism of ATP synthase
Stock, D., Gibbons, C., Aréchaga, I., Leslie, A. G. W., & Walker, J. E. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00147-0 · Cited by 325
Nishizaka, T., Oiwa, K., Noji, H., Kimura, S., Muneyuki, E., Yoshida, M., & Kinosita, K. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb721 · Cited by 276
Shimabukuro, K., Yasuda, R., Muneyuki, E., Hara, K. Y., Kinosita, K., & Yoshida, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2434983100 · Cited by 247
(1981) · International Journal of Biochemistry · doi:10.1016/0020-711x(81)90030-6 · Cited by 239
Jiang, W., Hermolin, J., & Fillingame, R. H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081424898 · Cited by 233
Stepping rotation of F 1 -ATPase visualized through angle-resolved single-fluorophore imaging
Adachi, K., Yasuda, R., Noji, H., Itoh, H., Harada, Y., Yoshida, M., & Kinosita, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.120174297 · Cited by 215
The rotary mechanism of the ATP synthase
Nakamoto, R. K., Scanlon, J. A. B., & Al‐Shawi, M. K. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.05.004 · Cited by 213
Self-citationGround State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 Aå Resolution
Bowler, M. W., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700203200 · Cited by 188
Evidence for rotation of V 1 -ATPase
Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., & Yokoyama, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0436796100 · Cited by 187
Interaction between Aldolase and Vacuolar H+-ATPase
Lu, M., Holliday, L. S., Li, Z., Dunn, W. A., & Gluck, S. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008768200 · Cited by 183
Direct Observation of the Rotation of ε Subunit in F1-ATPase
Kato‐Yamada, Y., Noji, H., Yasuda, R., Kinosita, K., & Yoshida, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19375 · Cited by 183
Bacterial Na+‐ATP synthase has an undecameric rotor
Stahlberg, H., Müller, D. J., Suda, K., Fotiadis, D., Engel, A. H., Meier, T. W., Matthey, U., & Dimroth, P. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve047 · Cited by 181
Holliday, L. S., Lu, M., Lee, B. S., Nelson, R. D., Solivan, S. M., Zhang, L., & Gluck, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004795200 · Cited by 173
The c15 ring of the Spirulina platensis F‐ATP synthase: F1/F0 symmetry mismatch is not obligatory
Pogoryelov, D., Yu, J., Meier, T. W., Vonck, J., Dimroth, P., & Müller, D. J. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400517 · Cited by 169
Cross, R. L., & Müller, V. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.065 · Cited by 168
Subunit Rotation of Vacuolar-type Proton Pumping ATPase
Hirata, T., Iwamoto-Kihara, A., Sun‐Wada, G., Okajima, T., Wada, Y., & Futai, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302756200 · Cited by 168
Self-citationProton Translocation by the F1FOATPase of Escherichia coli
Cain, B. D., & Simoni, R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94065-2 · Cited by 159
H+/ATP ratio of proton transport‐coupled ATP synthesis and hydrolysis catalysed by CF0F1—liposomes
Turina, P., Samoray, D., & Gräber, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg073 · Cited by 155
Mechanics of coupling proton movements to c‐ring rotation in ATP synthase
Fillingame, R. H., Angevine, C. M., & Dmitriev, O. Y. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01101-3 · Cited by 147
Rotation of the c subunit oligomer in fully functional F 1 F o ATP synthase
Tsunoda, S. P., Aggeler, R. J., Yoshida, M., & Capaldi, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.898 · Cited by 140
Omote, H., Sambonmatsu, N., Saito, K., Sambongi, Y., Iwamoto-Kihara, A., Yanagida, T., Wada, Y., & Futai, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.14.7780 · Cited by 133
Self-citationMitome, N., Suzuki, T., Hayashi, S., & Yoshida, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403545101 · Cited by 121
Sun‐Wada, G., Wada, Y., & Futai, M. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.04.013 · Cited by 119
Self-citationBörsch, M., Diez, M., Zimmermann, B., Reuter, R., & Gräber, P. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03198-8 · Cited by 119
Movements of the ε‐subunit during catalysis and activation in single membrane‐bound H+‐ATP synthase
Zimmermann, B., Diez, M., Zarrabi, N., Gräber, P., & Börsch, M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600682 · Cited by 107
Lightowlers, R. N., Howitt, S. M., Hatch, L. P., Gibson, F., & Cox, G. B. (1987) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(87)90118-6 · Cited by 104
Gogol, E. P., Johnston, E., Aggeler, R. J., & Capaldi, R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.24.9585 · Cited by 99
Nishio, K., Iwamoto-Kihara, A., Yamamoto, A., Wada, Y., & Futai, M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202149599 · Cited by 96
Self-citationFurther examination of seventeen mutations in Escherichia coli F1-ATPase beta-subunit.
Senior, A. E., & Al‐Shawi, M. K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36633-5 · Cited by 94
Rotation of the Proteolipid Ring in the V-ATPase
Yokoyama, K., Nakano, M., Imamura, H., Yoshida, M., & Tamakoshi, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303104200 · Cited by 90
Watts, S. D., Zhang, Y. E., Fillingame, R. H., & Capaldi, R. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00658-v · Cited by 88
KETCHUM, J. C., Al‐Shawi, M. K., & NAKAMOTO, K. R. (1998) · Biochemical Journal · doi:10.1042/bj3300707 · Cited by 83
Evidence for Structural Integrity in the Undecameric c-Rings Isolated from Sodium ATP Synthases
Meier, T. W., Matthey, U., von Ballmoos, C., Vonck, J., von Nidda, T. K., Kühlbrandt, W., & Dimroth, P. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01204-4 · Cited by 83
Stochastic High-speed Rotation of Escherichia coli ATP Synthase F1 Sector
Nakanishi‐Matsui, M., Kashiwagi, S., Hosokawa, H., Cipriano, D. J., Dunn, S. D., Wada, Y., & Futai, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510090200 · Cited by 77
Self-citationRotation scheme of V 1 -motor is different from that of F 1 -motor
Imamura, H., Takeda, M., Funamoto, S., Shimabukuro, K., Yoshida, M., & Yokoyama, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507764102 · Cited by 75
F0F1-ATPase gamma subunit mutations perturb the coupling between catalysis and transport.
Shin, K., Nakamoto, R. K., Maeda, M., & Futai, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36763-8 · Cited by 73
Self-citationRegulation and Reversibility of Vacuolar H+-ATPase
Hirata, T., Nakamura, N., Omote, H., Wada, Y., & Futai, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.386 · Cited by 73
Self-citationH(+)-ATPase gamma subunit of Escherichia coli. Role of the conserved carboxyl-terminal region.
Iwamoto, A., Miki, J., Maeda, M., & Futai, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34081-5 · Cited by 71
Self-citationNakamoto, R. K., Maeda, M., & Futai, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54014-x · Cited by 71
Self-citationF1-ATPase, Roles of Three Catalytic Site Residues
Löbau, S., Weber, J., Wilke-Mounts, S., & Senior, A. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3648 · Cited by 70
ATP Hydrolysis and Synthesis of a Rotary Motor V-ATPase from Thermus thermophilus
Nakano, M., Imamura, H., Toei, M., Tamakoshi, M., Yoshida, M., & Yokoyama, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801276200 · Cited by 70
Omote, H., Maeda, M., & Futai, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36724-9 · Cited by 69
Self-citationRotation of a Complex of the γ Subunit and c Ring of Escherichia coli ATP Synthase
Tanabe, M., Nishio, K., Iko, Y., Sambongi, Y., Iwamoto-Kihara, A., Wada, Y., & Futai, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100289200 · Cited by 64
Self-citationAl‐Shawi, M. K., Ketchum, C. J., & Nakamoto, R. K. (1997) · Biochemistry · doi:10.1021/bi971478r · Cited by 63
Self-citationAl‐Shawi, M. K., Ketchum, C. J., & Nakamoto, R. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2300 · Cited by 60
Self-citationIwamoto, A., Omote, H., Hanada, H., Tomioka, N., Itai, A., Maeda, M., & Futai, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55304-7 · Cited by 57
Self-citationOn what makes the γ subunit spin during ATP hydrolysis by F1
Ren, H., & Allison, W. S. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00075-x · Cited by 55
Rate Acceleration of ATP Hydrolysis by F1Fo-ATP Synthase
Senior, A. E., Nadanaciva, S., & Weber, J. (2000) · Journal of Experimental Biology · doi:10.1242/jeb.203.1.35 · Cited by 54
Role of the carboxyl terminal region of H+-ATPase (F0F1a subunit from Escherichia coli
Seiji, E. Y. A., Maeda, M., & Futai, M. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90265-k · Cited by 53
Self-citationNakamoto, R. K., Al‐Shawi, M. K., & Futai, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.14042 · Cited by 53
Self-citationIda, K., Noumi, T., Maeda, M., Fukui, T., & Futai, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67612-x · Cited by 50
Self-citationTemperature‐sensitive reaction intermediate of F1‐ATPase
Watanabe, R., Iino, R., Shimabukuro, K., Yoshida, M., & Noji, H. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401135 · Cited by 48
Synthase (H+ ATPase): coupling between catalysis, mechanical work, and proton translocation
Futai, M., Omote, H., Sambongi, Y., & Wada, Y. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00080-3 · Cited by 47
Self-citationPark, M.-Y., Omote, H., Maeda, M., & Futai, M. (1994) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124640 · Cited by 46
Self-citationOmote, H., Le, N. P., Park, M.-Y., Maeda, M., & Futai, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25656 · Cited by 41
Self-citationKanazawa, H., Hama, H., Rosen, B. P., & Futai, M. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90558-2 · Cited by 38
Self-citationAl‐Shawi, M. K., & Nakamoto, R. K. (1997) · Biochemistry · doi:10.1021/bi971477z · Cited by 37
Self-citationTemperature Dependence of the Rotation and Hydrolysis Activities of F1-ATPase
Furuike, S., Adachi, K., Sakaki, N., Shimo‐Kon, R., Itoh, H., Muneyuki, E., Yoshida, M., & Kinosita, K. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.123307 · Cited by 36
Nadanaciva, S., Weber, J., & Senior, A. E. (2000) · Biochemistry · doi:10.1021/bi000941o · Cited by 36
E., C., L., C., & Brini, M. (2004) · Wiley eBooks · doi:10.1002/3527606122 · Cited by 33
The Role of β-Arg-182, an Essential Catalytic Site Residue in Escherichia coli F1-ATPase
Nadanaciva, S., Weber, J., & Senior, A. E. (1999) · Biochemistry · doi:10.1021/bi990663x · Cited by 33
Determination of the Partial Reactions of Rotational Catalysis in F1-ATPase
Scanlon, J. A. B., Al‐Shawi, M. K., Le, N. P., & Nakamoto, R. K. (2007) · Biochemistry · doi:10.1021/bi700610m · Cited by 33
Self-citationYagi, H., Kajiwara, N., Iwabuchi, T., Izumi, K., Yoshida, M., & Akutsu, H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808212200 · Cited by 29
Rotational Catalysis of Escherichia coli ATP Synthase F1 Sector
Nakanishi‐Matsui, M., Kashiwagi, S., Ubukata, T., Iwamoto-Kihara, A., Wada, Y., & Futai, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700551200 · Cited by 28
Self-citationSekiya, M., Nakamoto, R. K., Al‐Shawi, M. K., Nakanishi‐Matsui, M., & Futai, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.009019 · Cited by 27
Self-citationStochastic proton pumping ATPases: From single molecules to diverse physiological roles
Nakanishi‐Matsui, M., & Futai, M. (2006) · IUBMB Life · doi:10.1080/15216540600702255 · Cited by 26
Self-citationStochastic rotational catalysis of proton pumping F-ATPase
Nakanishi‐Matsui, M., & Futai, M. (2008) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2008.2266 · Cited by 24
Self-citationA Rotor-Stator Cross-link in the F1-ATPase Blocks the Rate-limiting Step of Rotational Catalysis
Scanlon, J. A. B., Al‐Shawi, M. K., & Nakamoto, R. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804858200 · Cited by 21
Self-citationHayashi, K., Sun‐Wada, G., Wada, Y., Nakanishi‐Matsui, M., & Futai, M. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.06.011 · Cited by 17
Self-citationJones, P. C., Hermolin, J., & Fillingame, R. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.11355 · Cited by 15
Futai, M., Sun‐Wada, G., & Wada, Y. (2004) · doi:10.1002/3527606122.ch9 · Cited by 14
Self-citationATP-dependent Rotation of Mutant ATP Synthases Defective in Proton Transport
Hosokawa, H., Nakanishi‐Matsui, M., Kashiwagi, S., Fujii-Taira, I., Hayashi, K., Iwamoto-Kihara, A., Wada, Y., & Futai, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502650200 · Cited by 10
Self-citationKashiwagi, S., Iwamoto-Kihara, A., Kojima, M., Nonaka, T., Futai, M., & Nakanishi‐Matsui, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.157 · Cited by 10
Self-citationε-Binding regions of the γ subunit of Escherichia coli ATP synthase
Dunn, S. D. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(96)00159-4 · Cited by 10
Mutational analysis of F1F0 ATPase: catalysis and energy coupling.
Omote, H., & Futai, M. (1998) · PubMed · Cited by 5
Self-citationShin, J. M., Vagin, O., Simon, W. A., & Sachs, G. M. (2004) · Elsevier eBooks · doi:10.1016/b0-12-386860-2/00297-5 · Cited by 2
Cited by
Sorted by citations
Erbaş-Çakmak, S., Leigh, D. A., McTernan, C. T., & Nussbaumer, A. L. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00146 · Cited by 2,016
A thermo-physical analysis of the proton pump vacuolar-ATPase: the constructal approach
Lucia, U., Ponzetto, A., & Deisboeck, T. S. (2014) · Scientific Reports · doi:10.1038/srep06763 · Cited by 275
Enzyme Catalysis To Power Micro/Nanomachines
Ma, X., Hortelão, A. C., Patiño, T., & Sánchez, S. (2016) · ACS Nano · doi:10.1021/acsnano.6b04108 · Cited by 256
Receptor-mediated cell mechanosensing
Chen, Y., Ju, L. A., Rushdi, M. N., Ge, C., & Zhu, C. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-04-0228 · Cited by 242
Janus particles for biological imaging and sensing
Yi, Y., Sanchez, L., Gao, Y., & Yu, Y. (2016) · The Analyst · doi:10.1039/c6an00325g · Cited by 189
Metadata
- Authors
- Nakanishi-Matsui, M., Sekiya, M., Nakamoto, R. K., & Futai, M.
- Affiliations
- Iwate Medical University (JP)
- University of Virginia (US)
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2010-08
- Volume
- 1797
- Issue
- 8
- Pages
- 1343-1352
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2140969249
- Cited by
- 120
- References
- 103
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3 · 2023: 23 · 2022: 2 · 2021: 8 · 2020: 7 · 2019: 2 · 2018: 5 · 2017: 6 · 2016: 8 · 2015: 7 · 2014: 7 · 2013: 10 · 2012: 11
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1082 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- CREST (Core Research for Evolutional Science and Technology)
- JST (Japan Science and Technology Agency)
- Japanese Ministry of Education, Culture, and Science
- Terumo Life Science Foundation
- Japan Foundation for Applied Enzymology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Keywords
- F1-ATPase, V-ATPase, proton-pumping ATPase, ATP production, single-molecule FRET, Escherichia coli
- MeSH terms
- Adenosine Triphosphate, Animals, Catalysis, Proton-Translocating ATPases, Humans, Rotation, Thermodynamics, Vacuolar Proton-Translocating ATPases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
