作者: Christian Zscherp , Ramona Schlesinger , Joachim Heberle
关键词: Proton 、 Attenuated total reflection 、 Photochemistry 、 Bacteriorhodopsin 、 Mutant 、 Wild type 、 Chemistry 、 Protonation 、 Deprotonation 、 Catalytic cycle 、 Biophysics 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: The photoreaction of the E194Q mutant bacteriorhodopsin has been investigated at various pH values by time-resolved step-scan Fourier-transform infrared difference spectroscopy employing attenuated total reflection technique. spectrum 8.4 is comparable to N-BR spectra wild type with remarkable exception that D85 deprotonated. Since retinal configuration not perturbed mutation, it concluded there no interaction during lifetime N state. At 6, a consecutive state O intermediate detected in which D212 transiently protonated. comparison wild-type reveals protonation represents an step proton transfer from release group final stage reaction cycle. described effects are more pronounced than E204Q demonstrating different roles these two glutamates/glutamic acids least stages catalytic cycle bacteriorhodopsin.