{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,6]],"date-time":"2026-05-06T06:13:50Z","timestamp":1778048030584,"version":"3.51.4"},"reference-count":28,"publisher":"Springer Science and Business Media LLC","issue":"6796","license":[{"start":{"date-parts":[[2000,8,1]],"date-time":"2000-08-01T00:00:00Z","timestamp":965088000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2000,8]]},"DOI":"10.1038\/35020614","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T08:45:49Z","timestamp":1027673149000},"page":"653-657","source":"Crossref","is-referenced-by-count":397,"title":["Molecular mechanism of vectorial proton translocation by bacteriorhodopsin"],"prefix":"10.1038","volume":"406","author":[{"given":"Sriram","family":"Subramaniam","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard","family":"Henderson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","reference":[{"key":"BF35020614_CR1","doi-asserted-by":"publisher","first-page":"899","DOI":"10.1016\/S0022-2836(05)80271-2","volume":"213","author":"R Henderson","year":"1990","unstructured":"Henderson, R. et al. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213, 899\u2013929 (1990).","journal-title":"J. Mol. Biol."},{"key":"BF35020614_CR2","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1016\/S0959-440X(99)80065-7","volume":"9","author":"S Subramaniam","year":"1999","unstructured":"Subramaniam, S. The structure of bacteriorhodopsin: an emerging consensus. Curr. Opin. Struct. Biol. 9, 462\u2013468 (1999).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"BF35020614_CR3","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1006\/jmbi.1999.2589","volume":"287","author":"S Subramaniam","year":"1999","unstructured":"Subramaniam, S. et al. Protein conformational changes in the bacteriorhodopsin photocycle. J. Mol. Biol. 287, 145\u2013 161 (1999).","journal-title":"J. Mol. Biol."},{"key":"BF35020614_CR4","doi-asserted-by":"publisher","first-page":"2152","DOI":"10.1093\/emboj\/19.10.2152","volume":"19","author":"J Vonck","year":"2000","unstructured":"Vonck, J. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J. 19, 2152 \u20132160 (2000).","journal-title":"EMBO J."},{"key":"BF35020614_CR5","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1126\/science.286.5438.255","volume":"286","author":"H Luecke","year":"1999","unstructured":"Luecke, H., Schobert, B., Richter, H. -T., Cartailler, J. -P., & Lanyi, J. K. Structural changes in bacteriorhodopsin during ion transport at 2 \u00c5 resolution. Science 286, 255\u2013260 ( 1999).","journal-title":"Science"},{"key":"BF35020614_CR6","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1038\/35020607","volume":"406","author":"H-J Sass","year":"2000","unstructured":"Sass, H.-J. et al. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature 406, 649\u2013653 (2000).","journal-title":"Nature"},{"key":"BF35020614_CR7","doi-asserted-by":"publisher","first-page":"7876","DOI":"10.1073\/pnas.86.20.7876","volume":"86","author":"NA Dencher","year":"1989","unstructured":"Dencher, N. A., Dresselhaus, D., Zaccai, G. & B\u00fcldt, G. Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proc. Natl Acad. Sci. USA 86 , 7876\u20137879 (1989).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35020614_CR8","doi-asserted-by":"publisher","first-page":"521","DOI":"10.1002\/j.1460-2075.1991.tb07978.x","volume":"10","author":"MHJ Koch","year":"1991","unstructured":"Koch, M. H. J. et al. Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10, 521\u2013526 (1991).","journal-title":"EMBO J."},{"key":"BF35020614_CR9","doi-asserted-by":"publisher","first-page":"12282","DOI":"10.1021\/bi9712302","volume":"36","author":"H Kamikubo","year":"1996","unstructured":"Kamikubo, H. et al. The last phase of the reprotonation switch in bacteriorhodopsin: The transition between the M-type and the N-type protein conformation depends on hydration. Biochemistry 36, 12282\u2013 12287 (1996).","journal-title":"Biochemistry"},{"key":"BF35020614_CR10","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1002\/j.1460-2075.1993.tb05625.x","volume":"12","author":"S Subramaniam","year":"1993","unstructured":"Subramaniam, S., Gerstein, M., Oesterhelt, D. & Henderson, R. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12, 1\u20138 (1993).","journal-title":"EMBO J."},{"key":"BF35020614_CR11","doi-asserted-by":"publisher","first-page":"1018","DOI":"10.1016\/S0006-3495(99)77266-8","volume":"76","author":"T Oka","year":"1999","unstructured":"Oka, T. et al. Conformational change of helix G in the bacteriorhodopsin photocycle: Investigation with heavy atom labeling and X-ray diffraction. Biophys. J. 76, 1018\u20131023 (1999).","journal-title":"Biophys. J."},{"key":"BF35020614_CR12","doi-asserted-by":"publisher","first-page":"7097","DOI":"10.1021\/bi00418a064","volume":"27","author":"SP Fodor","year":"1988","unstructured":"Fodor, S. P. et al. Chromophore structure in bacteriorhodopsin's N intermediate: implications for the proton pumping mechanism. Biochemistry 27, 7097\u20137101 (1988).","journal-title":"Biochemistry"},{"key":"BF35020614_CR13","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1139\/v96-063","volume":"74","author":"GR Elia","year":"1996","unstructured":"Elia, G. R., Childs, R. F., Britten, J. F., Yang, D. S. C. & Santarsiero, B. D. Structure and wavelength modification in retinylidene iminium salts. Can. J. Chem. 74, 591\u2013601 (1996).","journal-title":"Can. J. Chem."},{"key":"BF35020614_CR14","doi-asserted-by":"publisher","first-page":"9416","DOI":"10.1021\/ja00181a067","volume":"112","author":"BD Santarsiero","year":"1990","unstructured":"Santarsiero, B. D., James, M. N. G., Mahendran, M. & Childs, R. F. The crystal structure of N-methyl-N-phenyl-retinylideneiminium perchlorate: a structural model for the bacteriorhodopsin chromophore. J. Am. Chem. Soc. 112, 9416\u20139418 (1990).","journal-title":"J. Am. Chem. Soc."},{"key":"BF35020614_CR15","doi-asserted-by":"publisher","first-page":"214","DOI":"10.1107\/S0567740872002092","volume":"28","author":"T Hamanaka","year":"1972","unstructured":"Hamanaka, T., Mitsui, T., Ashida, T. & Kakudo, M. The crystal structure of all-trans retinal1. Acta Crystallogr. B 28, 214\u2013222 ( 1972).","journal-title":"Acta Crystallogr."},{"key":"BF35020614_CR16","doi-asserted-by":"publisher","first-page":"2936","DOI":"10.1107\/S0567740872007253","volume":"28","author":"CH Stam","year":"1972","unstructured":"Stam, C. H. The crystal structure of a monoclinic modification and the refinement of a triclinic modification of vitamin A acid (retinoic acid), C20H 28O2. Acta Crystallogr. B 28, 2936\u20132945 (1972).","journal-title":"Acta Crystallogr. B"},{"key":"BF35020614_CR17","doi-asserted-by":"publisher","first-page":"2197","DOI":"10.1107\/S0567740881008388","volume":"37","author":"CJ Simmons","year":"1981","unstructured":"Simmons, C. J., Liu, R. S. H., Denny, M. & Seff, K. The crystal structure of 13-cis-retinal. The molecular structures of its 6-s-cis and 6-s-trans conformers. Acta Crystallogr. B 37 , 2197\u20132205 (1981).","journal-title":"Acta Crystallogr. B"},{"key":"BF35020614_CR18","doi-asserted-by":"publisher","first-page":"711","DOI":"10.1107\/S0108270186094829","volume":"42","author":"CJ Simmons","year":"1986","unstructured":"Simmons, C. J., Asato, A. E. & Liu, R. S. H. Structure of All-trans-3,4-didehydroretinal (retinal2). Acta Crystallogr. C 42, 711\u2013715 (1986).","journal-title":"Acta Crystallogr. C"},{"key":"BF35020614_CR19","doi-asserted-by":"publisher","first-page":"11762","DOI":"10.1021\/bi990593u","volume":"38","author":"S Moltke","year":"1999","unstructured":"Moltke, S. et al. The angles between the C-1-, C-5-, and C-9-methyl bonds of the retinylidene chromophore and the membrane normal increase in the M-intermediate of bacteriorhodopsin: Direct determination with solid-state H-2 NMR. Biochemistry 38, 11762\u201311772 (1999).","journal-title":"Biochemistry"},{"key":"BF35020614_CR20","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1021\/bi991106d","volume":"39","author":"JM Griffiths","year":"2000","unstructured":"Griffiths, J. M. et al. Structural investigation of the active site in bacteriorhodopsin: Geometric constraints on the roles of Asp-85 and Asp-212 in the proton pumping mechanism from solid-state NMR. Biochemistry 39, 362\u2013371 (2000).","journal-title":"Biochemistry"},{"key":"BF35020614_CR21","doi-asserted-by":"publisher","first-page":"5040","DOI":"10.1073\/pnas.94.10.5040","volume":"94","author":"LS Brown","year":"1997","unstructured":"Brown, L. S. et al. A local electrostatic change is the cause of the large scale protein conformation shift in bacteriorhodopsin. Proc. Natl Acad. Sci. USA 94, 5040\u20135044 ( 1997).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35020614_CR22","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/S0021-9258(18)34020-1","volume":"257","author":"B Schobert","year":"1982","unstructured":"Schobert, B. & Lanyi, J. K. Halorhodopsin is a light-driven chloride pump. J. Biol. Chem. 257, 306\u2013 313 (1982).","journal-title":"J. Biol. Chem."},{"key":"BF35020614_CR23","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1146\/annurev.biophys.26.1.223","volume":"26","author":"WD Hoff","year":"1997","unstructured":"Hoff, W. D., Jung, K. H. and Spudich, J. L. Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Ann. Rev. Biophys. Biomol. Struct. 26, 223\u2013258 (1997).","journal-title":"Ann. Rev. Biophys. Biomol. Struct."},{"key":"BF35020614_CR24","doi-asserted-by":"publisher","first-page":"12470","DOI":"10.1021\/bi960849l","volume":"35","author":"C Altenbach","year":"1996","unstructured":"Altenbach, C. et al. Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study. Biochemistry 35, 12470\u2013 12478 (1996).","journal-title":"Biochemistry"},{"key":"BF35020614_CR25","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1016\/S0304-3991(98)00056-4","volume":"75","author":"AR Faruqi","year":"1999","unstructured":"Faruqi, A. R., Henderson, R. & Subramaniam, S. Cooled CCD detector with tapered fibre optics for recording electron diffraction patterns. Ultramicroscopy 75, 235\u2013250 (1999).","journal-title":"Ultramicroscopy"},{"key":"BF35020614_CR26","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1006\/jmbi.1996.0328","volume":"259","author":"N Grigorieff","year":"1996","unstructured":"Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M. & Henderson, R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393\u2013421 (1996).","journal-title":"J. Mol. Biol."},{"key":"BF35020614_CR27","doi-asserted-by":"publisher","first-page":"905","DOI":"10.1107\/S0907444998003254","volume":"54","author":"AT Brunger","year":"1998","unstructured":"Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905\u2013921 (1998).","journal-title":"Acta Crystallogr. D"},{"key":"BF35020614_CR28","doi-asserted-by":"publisher","first-page":"11673","DOI":"10.1073\/pnas.95.20.11673","volume":"95","author":"LO Essen","year":"1998","unstructured":"Essen, L. O., Siegert, R., Lehmannn, W. D. & Oesterhelt, D. Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl Acad. Sci. USA 95, 11673 \u20131167 (1998).","journal-title":"Proc. Natl Acad. Sci. USA"}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/35020614.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/35020614","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/doifinder\/10.1038\/35020614","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"http:\/\/www.nature.com\/articles\/35020614.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,17]],"date-time":"2023-05-17T02:04:13Z","timestamp":1684289053000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/35020614"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2000,8]]},"references-count":28,"journal-issue":{"issue":"6796","published-print":{"date-parts":[[2000,8]]}},"alternative-id":["BF35020614"],"URL":"https:\/\/doi.org\/10.1038\/35020614","relation":{},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2000,8]]}}}