Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
摘要：
Much progress has been made in our understanding of water molecule reactions on surfaces, proton solvation in gas-phase water clusters and proton transfer through liquids. Compared with our advanced understanding of these physico-chemical systems, much less is known about individual water molecules and their cooperative behaviour in heterogeneous proteins during enzymatic reactions. Here we use time-resolved Fourier transform infrared spectroscopy (trFTIR) and in situ HO/HO exchange FTIR 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. Our findings support the emerging paradigm that intraprotein water molecules are as essential for biological functions as amino acids.
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关键词：
HYDROGEN-BONDED NETWORK ANGSTROM RESOLUTION STRUCTURAL-CHANGES ENERGY-STORAGE EXCESS PROTON IR-SPECTRA BACTERIORHODOPSIN DYNAMICS ASSIGNMENT MOLECULES
DOI：
10.1038/nature04231
被引量：
年份：
2006
Elsevier
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掌桥科研
万方医学
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