Abstract
We discuss to what extent recent vibrational spectra of 14-2H, 15-2H and 14,15-2H isotopically labelled L550 provide evidence for the occurrence of 13-cis, 14-s-trans or 13-cis, 14-s-cis chromophore structures in bacteriorhodopsin's photocycle. The discussion is based on a quantum chemical (MNDO) vibrational analysis of four molecular fragments as models for the retinal chromophore in bacteriorhodopsin.
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Dewar MJS, Thiel W (1977) Ground states of molecules. 38. The MNDO method. Approximations and parameters. J Am Chem Soc 99:4899–4907
Fodor SPA, Pollar WT, Gebhard R, van den Berg EMM, Lugtenburg J, Mathies RA (1988) Bacteriorhodopsins's L550 intermediate contains a C14−C15 s-trans retinal chromophore. Proc Natl Acad Sci USA 85:2156–2160
Furukawa Y, Takeuchi H, Harada I, Tasumi M (1983) Molecular force fields of s-trans-1,3-butadiene and the second stable conformer. Bull Chem Soc Jpn 56:392–399
Gerwert K, Siebert F (1986) Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals. EMBO J 5:805–811
Großjean MF, Tavan P (1988) Wavelength regulation in bacteriorhodopsin and halorhodopsin: A PPP-MRD-CI study of retinal dyes. J Chem Phys 88:4884–4896
López-Garriga JJ, Babcock GT, Harrison JF (1986a) Factors influencing the C−N stretching frequency in neutral and protonated Schiff's bases. J Am Chem Soc 108:7241–7251
López-Garriga JJ, Babcock GT, Harrison JF (1986b) Increase in the C−N stretching frequency upon complexation of trans-retinylidene-n-butylamine with general Lewis acids. J Am Chem Soc 108:7131–7133
López-Garriga JJ, Hanton S, Babcock GT, Harrison JF (1986c) Rehybridization of the C−N bond upon protonation of methylimine increases the C−N stretching force constant. J Am Chem Soc 108:7251–7254
Mathies RA, Fodor SPA, Smith SO, van den Berg EMM, Gebhard R, Lugtenburg J (1988) Determination of retinal chromophore structure in rhodopsins with resonance Raman spectroscopy. In: Schmid ED, Schneider FW, Siebert F (eds) Spectroscopy of biological molecules. Wiley, Chichester, pp 215–223
Nakanishi K, Balogh-Nair V, Arnaboldi M, Tsujimoto K, Honig B (1980) An external point-charge model for bacteriorhodopsin to account for its purple color. J Am Chem Soc 102:7945–7947
Orlandi G, Schulten k (1979) Coupling of stereochemistry and proton donor-acceptor properties of a Schiff base. A model of a light-driven proton pump. Chem Phys Lett 64:370–374
Panchenko YN (1975) A partial vibrational reassignment of 1,3,-butadiene. Spectrochim Acta 31A:1201–1206
Panchenko YN, Pulay P, Török F (1976) Prediction of vibrational spectra by the CNDO/2 force method. II. The calculation of vibrational frequencies of cis and trans forms of glyoxal, acrolein and 1,3 butadiene. J Mol Struct 34:283–289
Schulten K, Tavan P (1978) A mechanism for the light-driven proton pump of Halobacterium halobium. Nature 272: 85–86
Schulten K, Schulten Z, Tavan P (1984) An isomerization model for the pump cycle of bacteriorhodopsin. In: Bolis L, Helmreich EJM, Passow H (eds) Information and energy transduction in biological membranes. Allan R Liss, New York, pp 113–131
Smith SO, Hornung I, van der Steen R, Pardoen JA, Braiman MS, Lugtenburg J, Mathies R (1986) Are C14−C15 single bond isomerizaions of the retinal chromophore involved in the proton-pumping mechanism of bacteriorhodopsin? Proc Natl Acad Sci USA 83:967–971
Stoeckenius W, Bogomolni RA (1982) Bacteriorhodopsin and related pigments of halobacteria. Annu Rev Biochem 52: 587–616
Tavan P, Schulten K (1986) Evidence for a 13,14-cis cycle in bacteriorhodopsin. Biophys J 50:81–89
Tavan P, Schulten K, Oesterhelt D (1985) The effect of protonation and electrical interactions on the stereochemistry of retinal Schiff bases. Biophys J 47:415–430
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Großjean, M.F., Tavan, P. & Schulten, K. Can normal mode analysis reveal the geometry of the L550 chromophore of bacteriorhodopsin?. Eur Biophys J 16, 341–349 (1989). https://doi.org/10.1007/BF00257882
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DOI: https://doi.org/10.1007/BF00257882