A Local Electrostatic Change is the Cause of the Large-Scale Protein Conformation Shift in Bacteriorhodopsin

During light-driven proton transport bacteriorhodopsin shuttles between two protein conformations. A large-scale structural change similar to that in the photo-chemical cycle is produced in the D85N mutant upon raising the pH, even without illumination. We report here that (i) the pKa values for the...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1997-05, Vol.94 (10), p.5040-5044
Hauptverfasser:	Brown, Leonid S., Kamikubo, Hironari, Zimányi, László, Kataoka, Mikio, Tokunaga, Fumio, Verdegem, Peter, Lugtenburg, Johan, Lanyi, Janos K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteria Bacteriorhodopsins Bacteriorhodopsins - chemistry Bacteriorhodopsins - metabolism Biochemistry Biological Sciences Biology Biophysics Chromophores Crystallography, X-Ray Fourier transformations Halobacterium Hydrogen-Ion Concentration Ions Isomerism Isomerization Kinetics Light Mutagenesis, Site-Directed Photoexcitation Physics Point Mutation Protein Conformation Proteins Protons Recombinant Proteins - chemistry Recombinant Proteins - metabolism Retinaldehyde - metabolism Schiff Bases Spectrum Analysis, Raman Static Electricity
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