[1] Lanyi J K. Bacteriorhodopsin
[J] . Annu Rev Physiol, 2004 , 66 : 665 -688.


[2] Lanyi J K. Proton transfers in the bacteriorhodopsin photocycle
[J] . Biochim Biophys Acta, 2006 , 1757: 1012-1018.


[3] Neutze R. Pebay-Peyroula E, Edman K, et al. Bacteriorhodopsin: a high-resolution structural view of vectorial proton transport
[J] . Biochim Biophys Acta, 2002, 1565 : 144 -167.


[4] Wise K J, Gillespie NB, Stuart JA, et al. Optimization of bacteriorhodopsin for bioelectronic devices
[J] . Trends Biotechnol, 2002, 20: 387-394.


[5] Hoffmann M, Wanko M, Strodel P, et al. Color tuning in rhodopsins: the mechanism for the spectral shift between bacteriorhodopsin and sensory rhodopsin II
[J] . J Am Chem Soc, 2006 , 128 : 10808-10818.


[6] Mogi T, Stern L J, Marti T, et al. Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
[J] . Proc Natl Acad Sci USA, 1988, 85 : 4148- 4152 .


[7] Subramaniam S, Greenhalgh D A, Rath P, et al. Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal——— all-trans-retinal reisomerization
[J] . Proc Natl Acad Sci USA, 1991 , 88: 6873-6877.


[8] Luecke H, Schobert B, Richter H T, et al. Structure of bacteriorhodopsin at 1. 55A resolution
[J] . J Mol Biol, 1999, 291: 899-911.


[9] Luecke H, Schobert B, Cartailler J P, et al. Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin
[J] . J Mol Biol, 2000 , 300 : 1237-1255.


[10] Peck R F, DasSarma S, Krebs M P. Homologous gene knockout in the archaeon Halobacteriumsalinarumwith ura3 as a counterselectable marker
[J] . Mol Microbiol, 2000, 35 : 667 -676.


[11] Oesterhelt D, Stoeckenius W. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
[J] . Methods Enzymol, 1974, 31 : 667-678 .


[12] Radzwill N, Gerwert K, Steinhoff H J. Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
[J] . Biophys J, 2001, 80 : 2856-2866.


[13] Cao Y, Brown L S, Needleman R, et al. 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
[J] . Biochemistry, 1993, 32: 10239-10248 .


[14] Metz G, Siebert F, Engelhard M. Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation
[J] . FEBS Lett, 1992 , 303: 237-241.


[15] Zimanyi L, Cao Y, Chang M, et al. The two consecutive M substates in the photocycle of bacteriorhodopsin are affected specifically by the D85N and D96N residue replacements
[J] . Photochem Photobiol, 1992, 56: 1049 -1055 .


[16] Garczarek F, Brown L S, Lanyi J K, et al. Proton binding within a membrane protein by a protonated water cluster
[J] . Proc Natl Acad Sci USA, 2005 , 102 : 3633-3638.


[17] Yoshitsugu M, Shibata M, Ikeda D, et al. Color change of proteorhodopsin by a single amino acid replacement at a distant cytoplasmic loop
[J] . Angew Chem Int Ed Engl, 2008, 47: 3923-3926.