Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy

Article Abstract:

Time-resolved Fourier transform infrared spectroscopy and in situ H2 (super 18)O/H2 (super 16)O exchange FTIR is used to determine how the membrane protein bacteriorhodopsin uses the interplay among strongly hydrogen-bonded water molecules, a water molecule with a dangling hydroxyl group and a protonated water cluster to transfer protons. The precise arrangement of water molecules in the protein matrix results in a controlled Grotthuss proton transfer, in contrast to the random proton migration that occurs in liquid water.

Germany, Science & research, Analysis, Fourier transform infrared spectroscopy

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Bacteriorhodopsin as a model for proton pumps

Article Abstract:

The bacteriorhodopsin is the simplest proton pump which causes local changes at the active site on energization to influence the overall protein structure. In the mechanism of bacteriorhodopsin, the protein conformations are the carriers of electrons and hydrogen within the membrane phase. The active sites are translocated and the electrostatic interactions of the active sites are transformed by bringing conformational transition in the protein.

Electrostatics

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Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

Article Abstract:

Research is presented concerning the modeling of the light-driven, vectorial transport of protons by the membrane protein bacteriorhodopsin. The switch mechanism which allows pumping is discussed.

Letter to the Editor, Protons, Schiff bases

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