Mechanism of color tuning in proton transporter Bacteriorhodopsin

doi:10.7523/j.issn.2095-6134.2010.5.008

Abstract

Abstract:

The color tuning in Bacteriorhodopsin is mostly caused by mutated residues which directly interact with retinal. In the present study, we have found a significant color tuning at Ile78 substituted with a non-native residue R1. However, no color tuning at Gln75, Asn76, Thr128, Lys129, or Leu61 was observed. In Bacteriorhodopsin photocycle, the lifetime of M412 was significantly prolonged after the substitution. The structural analysis suggested that R1 might have a direct contact with the "water trimer" and interact with retinal through the long-distance hydrogen bonded network.

Key words: color tuning, retinal, proton transport, photocycle

CLC Number:

Q632

CHEN De-Liang, ZHAO Qian, HAN Rui. Mechanism of color tuning in proton transporter Bacteriorhodopsin[J]. , 2010, 27(5): 632-637.

References

[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.