Photobiophysics Publications

(Guelph Photobiophysics group members are underlined)

  • 138.Saliminasab M., Yamazaki Y., Palmateer A., Harris A., Schubert L., Langner P., Heberle J., Bondar A.-N., Brown L.S. (2023) A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins. J. Phys. Chem. B, in press.
  • 137. Morizumi T., Kim K., Li H., Govorunova E.G., Sineshchekov O.A., Wang Y., Zheng L., Bertalan É., Bondar A.N., Askari A., Brown L.S., Spudich J.L., Ernst O.P. (2023) Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting K+ and Na+ selectivities. Nat. Commun., 14: 4365.
  • 136. Govorunova E.G., Sineshchekov O.A., Brown L.S., Bondar A.-N., Spudich J.L. (2022) Structural foundations of potassium selectivity in channelrhodopsins. mBio, 13: e03039-22. 
  • 135. Sugiura M., Ishikawa K., Katayama K., Sumii Y., Abe-Yoshizumi R., Tsunoda S.P., Furutani Y., Shibata N., Brown L.S., Kandori H. (2022) Unusual Photoisomerization Pathway in a Near-Infrared Light Absorbing Enzymerhodopsin. J. Phys. Chem. Lett., 13: 9539−9543. 
  • 134.Malakar P., Das I., Bhattacharya S., Harris A., Sheves M., Brown L.S., Ruhman S. (2022) Bidirectional Photochemistry of Antarctic Microbial Rhodopsin: Emerging Trend of Ballistic Photoisomerization from the 13-cis Resting State. J. Phys. Chem. Lett., 13: 8134–8140. 
  • 133. Govorunova E.G., Sineshchekov O.A., Brown L.S., Spudich J.L. (2022) Biophysical Characterization of Light-Gated Ion Channels Using Planar Automated Patch Clamp. 
    Front. Mol. Neurosci., 15: 976910. 
  • 132.Govorunova E.G., Gou Y., Sineshchekov O.A., Li H., Lu X., Wang Y., Brown L.S., St-Pierre F., Xue M., Spudich J.L. (2022) Kalium channelrhodopsins are natural light-gated potassium channels that mediate optogenetic inhibition. Nat. Neurosci., 25: 967-974. 
  • 131.Lazaratos M., Siemers M., Brown L.S., Bondar A.-N. (2022) Conserved hydrogen-bond motifs of membrane transporters and receptors. Biochim. Biophys. Acta, 1864: 183896. 
  • 130. Brown L.S.(2022) Light-driven proton transfers and proton transport by microbial rhodopsins - A biophysical perspective. Biochim. Biophys. Acta, 1864: 183867. 
  • 129. Govorunova E.G., Sineshchekov O.A., Li H., Wang Y., Brown L.S, Palmateer A., Melkonian M., Cheng S., Carpenter E., Patterson J., Wong G.K., Spudich J.L. (2021) Cation and Anion Channelrhodopsins: Sequence Motifs and Taxonomic Distribution. mBio, 12: e01656-21. 
  • 128. Cheng Z., Mobley C., Misra S.K., Gadepalli R.S., Hammond R.I., Brown L.S, Rimoldi J.M., Sharp J.S. (2021) Self-Organized Amphiphiles Are Poor Hydroxyl Radical Scavengers in Fast Photochemical Oxidation of Proteins Experiments. J. Am. Soc. Mass Spectrom., 32:1155-1161. 
  • 127. Pfeuti G., Brown L.S, Erulin A., Selim K., Kütter M.T., Bureau D.P. (2021) Trans-gauche-trans disulphide conformers measured by means of FT-Raman may be predictors of apparent digestibility of crude protein in feather meal fed to rainbow trout (Oncorhynchus mykiss). Animal Feed Sci. Technol., 274: 114829.
  • 126. Govorunova E.G., Sineshchekov O.A., Li H., Wang Y., Brown L.S., Spudich J.L. (2020) RubyACRs, nonalgal anion channelrhodopsins with highly red-shifted absorption. Proc. Natl. Acad. Sci. USA, 117: 22833-22840. 
  • 125. Besaw J.E., Ou W.L., Morizumi T., Eger B.T., Sanchez Vasquez J.D., Chu J.H.Y., Harris A., Brown L.S., Miller R.J.D., Ernst O.P. (2020) The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants. J. Biol. Chem., 295: 14793-14804. 
  • 124. Harris A., Lazaratos M., Siemers M., Watt E., Hoang A., Tomida S., Schubert L., Saita M., Heberle J., Furutani Y., Kandori H., Bondar A.-N., Brown L.S. (2020) Mechanism of inward proton transport in an Antarctic microbial rhodopsin. J. Phys. Chem. B, 124: 4851-4872.
  • 123. de Vlugt J.E., Xiao P., Munro R., Charchoglyan A., Brewer D., Al-Abdul-Wahid M.S., Brown L.S., Ladizhansky V. (2020) Identifying lipids tightly bound to an integral membrane protein. Biochim. Biophys. Acta, 1862: 183345.
  • 122. Sineshchekov O.A., Govorunova E.G., Li H., Wang Y., Melkonian M., Wong G.K.-S., Brown L.S., Spudich J.L. (2020) Conductance mechanisms of rapidly desensitizing cation channelrhodopsins from cryptophyte algae. mBio, 11: e00657-20.
  • 121. Munro R.A., de Vlugt J., Ladizhansky V., Brown L.S. (2020) Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 in Pichia pastoris for Solid-State NMR. Biomolecules, 10: 434.
  • 120. Pfeuti G., Brown L.S., Longstaffe J.G., Peyronel F., Bureau D.P., Kiarie E.G. (2020) Predicting the standardized ileal digestibility of crude protein in feather meal fed to broiler chickens using a pH-stat and a FT-Raman method. Animal Feed Sci. Technol., 261: 114340.
  • 119. Siemers M., Lazaratos M., Karathanou K., Guerra F., Brown L.S., Bondar A.-N. (2019) Bridge: A Graph-Based Algorithm to Analyze Dynamic H-Bond Networks in Membrane Proteins. J. Chem. Theory Comput., 15: 6781-6798.
  • 118. Xiao P., Bolton D., Munro R.A., Brown L.S., Ladizhansky V. (2019) Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway. Nat. Commun., 10: 3867.
  • 117. Dingwell D., Brown L.S., Ladizhansky V. (2019) Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR Under Nearly Physiological Conditions. J. Phys. Chem. B, 123: 7700-7710.
  • 116. Morizumi T., Ou W.-L., Van Eps N., Inoue K., Kandori H., Brown L.S., Ernst O.P. (2019) X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin. Scientific Reports, 9: 11283. 
  • 115. Pfeuti G., Longstaffe J., Brown L.S., Shoveler A., Taylor C., Bureau D. (2019) Disulphide bonds and crosslinked amino acids may affect amino acid utilization in feather meal fed to rainbow trout (Oncorhynchus mykiss). Aquaculture Research, 50: 2081-2095.
  • 114. Good D.B., Voinov M.A., Bolton D., Ward M.E., Sergeyev I.V., Caporini M., Scheffer P., Lo A., Rosay M., Marek A., Brown L.S., Smirnov A.I., Ladizhansky V. (2019) A biradical-tagged phospholipid as a polarizing agent for solid-state MAS Dynamic Nuclear Polarization NMR of membrane proteins. Solid State Nucl. Magn. Reson., 100: 92-101.
  • 113. Munro R.A., de Vlugt J., Ward M.E., Kim S.Y., Lee K.A., Jung K.-H., Ladizhansky V., Brown L.S. (2019) Biosynthetic Production of Fully Carbon-13 Labeled Retinal in E. coli for Structural and Functional Studies of Rhodopsins. J. Biomol. NMR, 73: 49-58.
  • 112. Bolton D., Brown L.S., Ladizhansky V. (2018) Partial solid-state NMR 1H, 13C, 15N resonance assignments of a perdeuterated back-exchanged seven-transmembrane helical protein Anabaena Sensory Rhodopsin. Biomol. NMR Assign., 12: 237-242.
  • 111. Harris A., Saita M., Resler T., Hughes-Visentin A., Maia R., Sellnau F., Bondar A.-N., Heberle J., Brown L.S. (2018) Molecular details of the unique mechanism of chloride transport by a cyanobacterial rhodopsin. Phys. Chem. Chem. Phys., 20: 3184-3199.
  • 110. Brown L.S., Ernst O.P. (2017) Recent advances in biophysical studies of rhodopsins - oligomerization, folding, and structure. Biochim. Biophys. Acta, 1865: 1512-1521.
  • 109. Milikisiyants S., Wang S., Munro R.A., Donohue M., Ward M.E., Bolton D., Brown L.S., Smirnova T.I., Ladizhansky V., Smirnov A.I. (2017) Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints. J. Mol. Biol., 429: 1903-1920.
  • 108. Yoshida K., Tsunoda S.P., Brown L.S., Kandori H. (2017) A unique choanoflagellate enzyme rhodopsin with cyclic nucleotide phosphodiesterase activity. J. Biol. Chem., 292: 7531-7541.
  • 107. Wang S., Ing C., Emami S., Jiang Y., Liang H., Pomes R., Brown L.S., Ladizhansky V. (2016) Structure and Dynamics of Extracellular Loops in Human Aquaporin-1 from Solid-State NMR and Molecular Dynamics. J. Phys. Chem. B., 120: 9887-9902.
  • 106. Ward M., Ladizhansky V., Brown, L.S. (2016). Sample preparation of rhodopsins in the E. coli membrane for in situ Magic Angle Spinning Solid-State Nuclear Magnetic Resonance studies. Springer Protocols Handbook, Chemical and Synthetic Approaches in Membrane Biology: 253-267.
  • 105. Liu J., Liu C., Fan Y., Munro R.A., Ladizhansky V., Brown L.S., Wang S. (2016) Sparse 13C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins. J. Biomol. NMR, 65: 7-13.
  • 104. Ward M.E., Ritz E., Ahmed M.A., Bamm V.V., Harauz G., Brown L.S., Ladizhansky V. (2015) Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins. J. Biomol. NMR, 63: 375-388.
  • 103. Harris A., Ljumovic M., Bondar A.-N., Shibata Y., Ito S., Inoue K., Kandori H., Brown L.S. (2015) A new group of eubacterial light-driven retinal-binding proton pumps with an unusual cytoplasmic proton donor. Biochim. Biophys. Acta, 1847: 1518-1529.
  • 102. Voinov M.A., Good D.B., Ward M.E., Milikisiyants S., Marek A., Caporini M.A., Rosay M., Munro R.A., Ljumovic M., Brown L.S., Ladizhansky V., Smirnov A.I. (2015) Cysteine-specific labeling of proteins with a nitroxide biradical for Dynamic Nuclear Polarization NMR. J. Phys. Chem. B., 119: 10180-10190.
  • 101. Fan Y., Emami S., Munro R., Ladizhansky V., Brown L.S. (2015) Isotope labeling of eukaryotic membrane proteins in yeast for solid-state NMR. Meth. Enzymol., 565: 193-212.
  • 100. Brown L.S., Ladizhansky V. (2015) Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy. Protein Science, 24: 1333-1346.
  • 99. Ward M.E., Wang S., Munro R., Ritz E., Hung I., Gor'kov P.L., Jiang Y., Liang H., Brown L.S., Ladizhansky V. (2015) In situ structural studies of Anabaena sensory rhodopsin in the E. coli membrane. Biophys. J., 108: 1683-1696.
  • 98. Ward M.E., Brown L.S., Ladizhansky V. (2015) Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: application to Anabaena sensory rhodopsin. J. Magn. Reson., 253: 119-128.
  • 97. Choi A.R., Shi L., Brown L.S., Jung K.-H. (2014) Cyanobacterial light-driven proton pump, Gloeobacter rhodopsin: complementarity between rhodopsin-based energy production and photosynthesis. PLoS One, 9: e110643.
  • 96. Johnson P.J., Halpin A., Morizumi T., Brown L.S., Prokhorenko V., Ernst O.P., Miller R.J.D. (2014). The photocycle and ultrafast vibrational dynamics of bacteriorhodopsin in lipid nanodiscs. Phys. Chem. Chem. Phys., 16: 21310-21320.
  • 95. Brown L.S. (2014) Proton-pumping microbial rhodopsins - ubiquitous structurally simple helpers of respiration and photosynthesis. Chapter in The Structural Basis of Biological Energy Generation; Advances in Photosynthesis and Respiration, Springer, 39: 1-20.
  • 94. Good D.B., Wang S., Ward M.E., Struppe J.O., Brown L.S., Lewandowski J.R., Ladizhansky V. (2014) Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR. J. Am. Chem. Soc., 136: 2833-2842.
  • 93. Kuang L., Fernandes D.A., O'Halloran M., Zheng W., Jiang Y., Ladizhansky V., Brown L.S., Liang H. (2014) "Frozen" block copolymer nanomembranes with light-driven proton pumping performance, ACS Nano, 8: 537-545.
  • 92. Ward M.E., Wang S., Krishnamurthy S., Hutchins H., Fey M., Brown L.S., Ladizhansky V. (2014) High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning, J. Biomol. NMR, 58: 37-47.
  • 91. Ernst O.P., Lodowski D.T., Elstner M., Hegemann P., Brown L.S., Kandori H. (2014) Microbial and animal rhodopsins: structures, functions and molecular mechanisms. Chem. Rev., 114: 126-163.
  • 90. Brown L.S. (2014) Eubacterial rhodopsins - unique photosensors and diverse ion pumps. Biochim. Biophys. Acta, 1837: 553-561.
  • 89. Wang S., Munro R., Shi L., Kawamura I., Okitsu T., Wada A., Kim S.Y., Jung K.-H., Brown L.S., Ladizhansky V. (2013) Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein, Nature Methods, 10: 1007-1012.
  • 88. Brown L.S. (2013) A thin line between channels and pumps. Biophys. J., 104: 739-740.
  • 87. Emami S., Fan Y., Munro R., Ladizhansky V., Brown L.S. (2013) Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra. J. Biomol. NMR, 55: 147-155.
  • 86. Wang S., Shi L., Okitsu T., Wada A., Brown L.S., Ladizhansky V. (2013) Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin. Biomol. NMR Assign., 7: 253-256.
  • 85. Khanal A., Pan Y., Brown L.S., Konermann L. (2012) Pulsed hydrogen/deuterium exchange mass spectrometry for time-resolved membrane protein folding studies. J. Mass Spectrom., 47: 1620-1626.
  • 84. Wang S., Munro R., Kim S.Y., Jung K.-H., Brown L.S., Ladizhansky V. (2012) Paramagnetic relaxation enhancement reveals oligomerization interface of a membrane protein. J. Am. Chem. Soc., 134: 16995-16998.
  • 83. Ito H., Sumii M., Kawanabe A., Fan Y., Furutani Y., Brown L.S., Kandori H. (2012) Comparative FTIR study of a new fungal rhodopsin. J. Phys. Chem. B., 116: 11881-11889.
  • 82. Pan Y., Brown L.S., Konermann L. (2011) Hydrogen exchange mass spectrometry of bacteriorhodopsin reveals light-induced changes in the structural dynamics of a biomolecular machine. J. Am. Chem. Soc., 133: 20237-20244.
  • 81. Ward M.E., Shi L., Lake E.M., Krishnamurthy S., Hutchins H., Brown L.S., Ladizhansky V. (2011) Proton detected solid-state NMR reveals intramembrane polar networks in a seven-helical transmembrane protein proteorhodopsin. J. Am. Chem. Soc., 133: 17434-17443.
  • 80. Fan Y., Solomon P., Oliver R.P., Brown L.S. (2011) Photochemical characterization of a novel fungal rhodopsin from Phaeosphaeria nodorum. Biochim. Biophys. Acta, 1807: 1457-1466.
  • 79. Wang S., Shi L., Kawamura I., Brown L.S., Ladizhansky V. (2011) Site-specific solid-state NMR detection of hydrogen-deuterium exchange reveals conformational changes in a 7-helical transmembrane protein. Biophys. J., 101: L23-L25.
  • 78. Wang S., Kim S.Y., Jung K.-H., Ladizhansky V., Brown L.S. (2011) A eukaryotic-like interaction of soluble cyanobacterial sensory rhodopsin transducer with DNA. J. Mol. Biol., 411: 449-462.
  • 77. Pan Y., Brown L.S., Konermann L. (2011) Kinetic folding mechanism of an integral membrane protein examined by pulsed oxidative labeling and mass spectrometry. J. Mol. Biol., 410: 146-158.
  • 76. Pan Y., Brown L.S., Konermann L. (2011) Hydrogen/Deuterium exchange mass spectrometry and optical spectroscopy as complementary tools for studying the structure and dynamics of a membrane protein. Int. J. Mass Spectrom., 302: 3-11.
  • 75. Prokhorenko V.I., Halpin A., Johnson P.J.M., Miller R.J.D., Brown L.S. (2011) Coherent control of the isomerization of retinal in bacteriorhodopsin in the high intensity regime. J. Chem. Phys., 134: 085105.
  • 74. Fan Y., Shi L., Ladizhansky V., Brown L.S. (2011) Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment. J. Biomol. NMR, 49: 151-161.
  • 73. Shi L., Kawamura I., Jung K.-H., Brown L.S., Ladizhansky V. (2011) Conformation of a seven-helical transmembrane photosensor in the lipid environment. Angew. Chem. Int. Ed. Engl., 50: 1302-1305.
  • 72. Pan Y., Brown L.S., Konermann L. (2010) Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry. J. Am. Soc. Mass Spectrom., 21: 1947-1956.
  • 71. Pan Y., Brown L.S., Konermann L. (2009) Mapping the structure of an integral membrane protein under semi-denaturing conditions by laser-induced oxidative labeling and mass spectrometry. J. Mol. Biol., 394: 968-981.
  • 70. Shi L., Lake E., Ahmed M.A.M., Brown L.S., Ladizhansky V. (2009) Solid-state NMR study of proteorhodopsin in the lipid environment: secondary structure and dynamics. Biochim. Biophys. Acta, 1788: 2563-2574.
  • 69. Shi L., Ahmed M.A.M., Zhang W., Whited G., Brown L.S., Ladizhansky V. (2009) Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump - structural insights. J. Mol. Biol., 386: 1078-1093.
  • 68. Miranda M.R.M., Choi A.R., Shi L., Bezerra A.G., Jr., Jung K.-H., Brown L.S. (2009) The photocycle and proton translocation pathway in a cyanobacterial ion-pumping rhodopsin. Biophys. J., 96: 1471-1481.
  • 67. Ahmed M.A., Bamm V.V., Shi L., Steiner-Mosonyi M., Dawson J.F., Brown L.S., Harauz G., Ladizhansky V. (2009) Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin. Biophys. J., 96: 180-191.
  • 66. Pan Y., Stocks B.B., Brown L.S., Konermann L. (2009) Structural characterization of an integral membrane protein in its natural lipid environment by oxidative methionine labeling and mass spectrometry. Analyt. Chem., 81: 28-35.
  • 65. Shi L., Peng X., Ahmed M.A.M., Edwards D., Brown L.S., Ladizhansky V. (2008) Resolution enhancement by homonuclear J-decoupling: application to three-dimensional solid-state magic angle spinning NMR spectroscopy. J. Biomol. NMR,41: 9-15.
  • 64. Kim S.Y., Waschuk S.A., Brown L.S., Jung K.-H. (2008) Screening and characterization of proteorhodopsin color-tuning mutations in Escherichia coli with endogenous retinal synthesis. Biochim. Biophys. Acta, 1777: 504-513.
  • 63. Prokhorenko V.I., Nagy A.M., Brown L.S., Miller R.J.D. (2007) On the mechanism of weak-field coherent control of retinal isomerization in bacteriorhodopsin. Chem. Phys., 341: 296-309.
  • 62. Magyari K., Simon V., Fan Y., Brown L.S., Varo G. (2007) Absorption kinetics and electrical signals measured on Leptosphaeria rhodopsin. Digest J. Nanomaterials and Biostructures, 2: 265-269. 
  • 61. Fan Y., Shi L., Brown L.S. (2007) Structural basis of diversification of fungal retinal proteins probed by site-directed mutagenesis of Leptosphaeria rhodopsin. FEBS Lett., 581: 2557-2561.
  • 60. Furutani Y., Sumii M., Fan Y., Shi L., Waschuk S.A., Brown L.S., Kandori H. (2006) Conformational coupling between the cytoplasmic carboxylic acid and the retinal in a fungal light-driven proton pump. Biochemistry, 45: 15349-15358.
  • 59. Prokhorenko V.I., Nagy A.M., Brown L.S., Miller R.D. (2006) Experimental coherent control of retinal isomerization in bacteriorhodopsin. Springer Ser. Chem. Phys., 88: 462-464.
  • 58. Prokhorenko V.I., Nagy A.M., Waschuk S.A., Brown L.S., Birge R.R., Miller R.J.D. (2006) Coherent control of the retinal isomerization in bacteriorhodopsin. Science, 313: 1257-1261. Also see the discussion in 317: 453c.
  • 57. Shi L., Yoon S.R., Bezerra A.G., Jr., Jung K.-H., Brown L.S. (2006) Cytoplasmic shuttling of protons in Anabaena sensory rhodopsin: implications for signaling mechanism. J. Mol. Biol., 358: 686-700.
  • 56. Zimanyi L., Saltiel J., Brown L.S., Lanyi J.K. (2006) A priori resolution of the intermediate spectra in the bacteriorhodopsin photocycle: the time evolution of the L spectrum revealed. J. Phys. Chem. A, 110: 2318-2321.
  • 55. Brown L.S., Jung K.-H. (2006) Bacteriorhodopsin-like proteins of eubacteria and fungi: the extent of conservation of the haloarchaeal proton-pumping mechanism. Photochem. Photobiol. Sci., 5: 538-546.
  • 54. Sumii M., Furutani Y., Waschuk S.A., Brown L.S., Kandori H. (2005) Strongly hydrogen-bonded water molecule present near the retinal chromophore of Leptosphaeria rhodopsin, the bacteriorhodopsin-like proton pump from a eukaryote. Biochemistry, 44: 15159-15166.
  • 53. Waschuk S.A., Bezerra A.G., Jr., Shi L., Brown L.S. (2005) Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eucaryote. Proc. Natl. Acad. Sci. USA, 102: 6879-6883.
  • 52. Garczarek F., Brown L.S., Lanyi J.K., Gerwert K. (2005) Proton binding within a membrane protein by a protonated water cluster. Proc. Natl. Acad. Sci. USA, 102: 3633-3638.
  • 51. Furutani Y., Bezerra A.G., Jr., Waschuk S., Sumii M., Brown L.S., Kandori H. (2004) FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, the protein, and the water molecules after photoisomerization. Biochemistry, 43: 9636 -9646.
  • 50. Brown L.S. (2004) Fungal rhodopsins and opsin-related proteins: eukaryotic homologues of bacteriorhodopsin with unknown functions. Photochem. Photobiol. Sci., 3: 555-565.
  • 49. Schobert B., Brown L.S., Lanyi J.K. (2003) Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between asp-96 and the retinal Schiff base. J. Mol. Biol., 330: 553-570.
  • 48. Varo G., Brown L.S., Lakatos M., Lanyi J.K. (2003) Characterization of the photochemical reaction cycle of proteorhodopsin. Biophys. J., 84: 1202-1207.
  • 47. Dioumaev A.K., Brown L.S., Shih J., Spudich E.N., Spudich J.L., Lanyi J.K. (2002) Proton transfers in the photochemical reaction cycle of proteorhodopsin. Biochemistry, 41: 5348-5358. 
  • 46. Brown L.S., Needleman R., Lanyi J.K. (2002) Conformational change of the E-F interhelical loop in the M photointermediate of bacteriorhodopsin. J. Mol. Biol., 317: 471-478. 
  • 45. Dioumaev A.K., Brown L.S., Needleman R., Lanyi J.K. (2001) Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of Asp-96 in the N photointermediate of bacteriorhodopsin. Biochemistry, 40: 11308-11317. 
  • 44. Brown L.S. (2001) Proton transport mechanism of bacteriorhodopsin as revealed  by site-specific mutagenesis and protein sequence variability. Biochemistry (Moscow), 66: 1546-1554. 
  • 43. Brown L.S., Dioumaev A.K., Lanyi J.K., Spudich E.N., Spudich J.L. (2001) Photochemical reaction cycle and proton transfers in Neurospora rhodopsin. J. Biol. Chem., 276: 32495-32505. 
  • 42. Xiao W., Brown L.S., Needleman R., Lanyi J.K., Shin Y.-K. (2000) Light-induced rotation of a transmembrane a-helix in bacteriorhodopsin. J. Mol. Biol., 304: 715-721. 
  • 41. Brown L.S. (2000) Reconciling crystallography and mutagenesis: a synthetic approach to the creation of a comprehensive model for proton pumping by bacteriorhodopsin. Biochim. Biophys. Acta, 1460: 49-59. 
  • 40. Brown L.S., Needleman R., Lanyi J.K. (2000) Origins of deuterium kinetic isotope effects on the proton transfers of the bacteriorhodopsin photocycle. Biochemistry, 39: 938-945. 
  • 39. Dioumaev A.K., Brown L.S., Needleman R., Lanyi J.K. (1999) FTIR spectra of a late intermediate of the bacteriorhodopsin photocycle suggest transient protonation of Asp-212. Biochemistry, 38: 10070-10078. 
  • 38. Varo G., Brown L.S., Needleman R., Lanyi J.K. (1999) Binding of calcium ions to bacteriorhodopsin. Biophys. J., 76: 3219-3226. 
  • 37. Brown L.S., Needleman R., Lanyi J.K. (1999) Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin. Biochemistry, 38: 6855-6861. 
  • 36. Subramaniam S., Lindahl M., Bullough P., Faruqi A.R., Tittor J., Oesterhelt D., Brown L.S., Lanyi J., Henderson R. (1999) Protein conformational changes in the bacteriorhodopsin photocycle. J. Mol. Biol., 287: 145-161. 
  • 35. Brown L.S., Dioumaev A.K., Needleman R., Lanyi J.K. (1998) Connectivity of the retinal Schiff base to Asp-85 and Asp-96 during the bacteriorhodopsin photocycle: the local-access model. Biophys. J., 75: 1455-1465. 
  • 34. Dioumaev A.K., Brown L.S., Needleman R., Lanyi J.K. (1998) Partitioning of free energy gain between the photoisomerized retinal and the protein in bacteriorhodopsin. Biochemistry, 37: 9889-9893. 
  • 33. Brown L.S., Dioumaev A.K., Needleman R., Lanyi J.K. (1998) Local-access model for proton transfer in bacteriorhodopsin. Biochemistry, 37: 3982-3993. 
  • 32. Dioumaev A.K., Richter H.-T., Brown L.S., Tanio M., Tuzi S., Saito H., Kimura Y., Needleman R., Lanyi J.K. (1998) Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry, 37: 2496-2506. 
  • 31. Thorgeirsson T.E., Xiao W., Brown L.S., Needleman R., Lanyi J.K., Shin Y.-K. (1997) Transient channel-opening in bacteriorhodopsin: an EPR study. J. Mol. Biol., 273: 951-957. 
  • 30. Renthal R., Chung Y.-J., Escamilla R., Brown L.S., Lanyi J.K. (1997) Guanidinium restores the chromophore but not rapid proton release in bacteriorhodopsin mutant R82Q. Biophys. J., 73: 2711-2717. 
  • 29. Brown L.S., Kamikubo H., Zimanyi L., Kataoka M., Tokunaga F., Verdegem P., Lugtenburg J., Lanyi J.K. (1997) A local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA, 94: 5040-5044. 
  • 28. Kandori H., Yamazaki Y., Hatanaka M., Needleman R., Brown L.S., Richter H.-T., Lanyi J.K., Maeda A. (1997) Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin. Biochemistry, 36: 5134-5141. 
  • 27. Brown L.S., Needleman R., Lanyi J.K. (1996) Interaction of proton and chloride transfer pathways in recombinant bacteriorhodopsin with chloride transport activity: implications for the chloride translocation mechanism. Biochemistry, 35: 16048-16054. 
  • 26. Chon Y.-S., Sasaki J., Kandori H., Brown L.S., Lanyi J.K., Needleman R., Maeda A. (1996) Hydration of the counterion of the Schiff base in the  chloride transporting mutant of bacteriorhodopsin: FTIR and FT-Raman studies on the effect of anion binding when Asp85 is replaced with a neutral residue. Biochemistry, 35: 14244-14250. 
  • 25. Weidlich O., Schalt B., Friedman N., Sheves M., Lanyi J.K., Brown L.S.,  Siebert F. (1996) Steric interaction between the 9-methyl group of the retinal and tryptophan 182 controls 13-cis to all-trans reisomerization and proton uptake in the bacteriorhodopsin photocycle. Biochemistry, 35: 10807-10814. 
  • 24. Varo G., Brown L.S., Needleman R., Lanyi J.K. (1996) Proton transport by halorhodopsin. Biochemistry, 35: 6604-6611. 
  • 23. Richter H.-T., Brown L.S., Needleman R., Lanyi J.K. (1996) A linkage of the pKa's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry, 35: 4054-4062. 
  • 22. Brown L.S., Lanyi J.K. (1996) Determination of the transiently lowered pKa of the retinal Schiff base during the photocycle of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA, 93: 1731-1734. 
  • 21. Brown L.S., Sasaki J., Kandori H., Maeda A., Needleman R., Lanyi J.K. (1995) Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin. J. Biol. Chem., 270: 27122-27126. 
  • 20. Varo G., Brown L.S., Sasaki J., Kandori H., Maeda A., Needleman R., Lanyi J.K. (1995) Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle. Biochemistry, 34: 14490-14499. 
  • 19. Brown L.S., Varo G., Needleman R., Lanyi J.K. (1995) Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle. Biophys. J., 69:2103-2111. 
  • 18. Brown L.S., Varo G., Hatanaka M., Sasaki J., Kandori H., Maeda A., Friedman N., Sheves M., Needleman R., Lanyi J.K. (1995) The complex extracellular domain regulates the transient deprotonation and reprotonation of the retinal Schiff base during the bacteriorhodopsin photocycle. Biochemistry, 34: 12903-12911. 
  • 17. Sasaki J., Brown L.S., Chon Y.-S., Kandori H., Maeda A., Needleman R., Lanyi J.K. (1995) Conversion of bacteriorhodopsin into a chloride ion pump. Science, 269: 73-75. 
  • 16. Cao Y., Brown L.S., Sasaki J., Maeda A., Needleman R., Lanyi J.K. (1995) Relationship of proton release at the extracellular surface to deprotonation of the Schiff base in the bacteriorhodopsin photocycle. Biophys. J., 68: 1518-1530.
  • 15. Yamazaki Y., Sasaki J., Hatanaka M., Kandori H., Maeda A., Needleman R., Shinada T., Yoshihara K., Brown L.S., Lanyi J.K. (1995) Interaction of tryptophan-182 with the retinal 9-methyl group in the L intermediate of bacteriorhodopsin. Biochemistry, 34: 577-582.
  • 14. Brown L.S., Gat Y., Sheves M., Yamazaki Y., Maeda A., Needleman R., Lanyi J.K. (1994) The retinal Schiff base - counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85. Biochemistry, 33: 12001-12011.
  • 13. Kataoka M., Kamikubo H., Tokunaga F., Brown L.S., Yamazaki Y., Maeda A., Sheves M., Needleman R., Lanyi J.K. (1994) Energy coupling in an ion pump: the reprotonation switch of bacteriorhodopsin. J. Mol. Biol., 243: 621-638.
  • 12. Brown L.S., Yamazaki Y., Maeda A., Sun L., Needleman R., Lanyi J.K. (1994) The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues. J. Mol. Biol., 239: 401-414.
  • 11. Cao Y., Brown L.S., Needleman R., Lanyi J.K. (1993) Relationship of proton uptake on the cytoplasmic surface and reisomerization of the retinal in the bacteriorhodopsin photocycle: an attempt to understand the complex kinetics of the pH changes and the N and O intermediates. Biochemistry, 32: 10239-10248.
  • 10. Brown L.S., Zimanyi L., Needleman R., Ottolenghi M., Lanyi J.K. (1993) Photoreaction of the N intermediate of bacteriorhodopsin, and its relationship to the decay kinetics of the M intermediate. Biochemistry, 32: 7679-7685.
  • 9. Brown L.S., Bonet L., Needleman R., Lanyi J.K. (1993) Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle. Biophys. J., 65: 124-130.
  • 8. Brown L.S., Chamorovsky S.K. (1993) Light adaptation blockage in dehydrated purple membrane does not result from retinal isomerization inhibition. J. Photochem. Photobiol. B., 18: 123-126.
  • 7. Kononenko A.A., Lukashev E.P., Brown L.S., Chamorovsky S.K., Kruming B.A., Yakushev S.A. (1993) Model devices based on bacteriorhodopsin - prototypes of position sensitive photodetectors. Biophysics (Russia), 38: 996-1002.  
  • 6. Brown L.S., Druzhko A.B., Kononenko A.A., Chamorovsky S.K., Shakhbazyan V.Y. (1993) Spectral properties of bacteriorhodopsin analog obtained by reconstitution of bacterioopsin with 4-keto-retinal in vivo. Biol. Membr. (Russia), 10: 140-144.
  • 5. Brown L.S., Druzhko A.B., Chamorovsky S.K. (1992) The light adaptation of bacteriorhodopsin analog with 4-keto-retinal. Biophysics (Russia), 37: 59-65.  
  • 4. Brown L.S., Druzhko A.B., Lukashev E.P., Chamorovsky S.K. (1991) Investigation of the photochemical cycle of a bacteriorhodopsin analog containing 4-keto-retinal residue. Biol. Membr. (USSR), 8: 460-467. 
  • 3. Brown L.S., Semin B.K., Ivanov I.I., Kononenko A.A., Chamorovsky S.K., Churin A.A. (1991) Tetracaine induces the formation of the spectral form of bacteriorhodopsin BR-470 in purple membranes of halobacteria. Biochemistry (USSR), 56: 241-249. 
  • 2. Brown L.S., Kononenko A.A., Protasova T.B., Fedorovich I.B., Chamorovsky S.K. (1990) Effects of the ultraviolet radiation on bacteriorhodopsin. Radiobiol. (USSR), 30: 506-511. 
  • 1. Chamorovsky S.K., Sabo J., Brown L.S. The automated pulse laser spectrophotometer to investigate processes of a photoinduced charge transfer in photosynthesis (1989) Biol. Sci. (USSR), 6: 98-100.