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Low-temperature FTIR spectroscopy provides evidence for protein-bound water molecules in eubacterial light-driven ion pumps

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Abstract

Light-driven H+, Na+ and Cl pumps have been found in eubacteria, which convert light energy into a transmembrane electrochemical potential. A recent mutation study revealed asymmetric functional conversion between the two pumps, where successful functional conversions are achieved exclusively when mutagenesis reverses the evolutionary amino acid sequence changes. Although this fact suggests that the essential structural mechanism of an ancestral function is retained even after gaining a new function, questions regarding the essential structural mechanism remain unanswered. Light-induced difference FTIR spectroscopy was used to monitor the presence of strongly hydrogen-bonded water molecules for all eubacterial H+, Na+ and Cl pumps, including a functionally converted mutant. This fact suggests that the strongly hydrogen-bonded water molecules are maintained for these new functions during evolution, which could be the reason for successful functional conversion from Na+ to H+, and from Cl to H+ pumps. This also explains the successful conversion of the Cl to the H+ pump only for eubacteria, but not for archaea. It is concluded that water-containing hydrogen-bonding networks constitute one of the essential structural mechanisms in eubacterial light-driven ion pumps.

Graphical abstract: Low-temperature FTIR spectroscopy provides evidence for protein-bound water molecules in eubacterial light-driven ion pumps

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Publication details

The article was received on 19 Aug 2017, accepted on 22 Sep 2017 and first published on 22 Sep 2017


Article type: Paper
DOI: 10.1039/C7CP05674E
Citation: Phys. Chem. Chem. Phys., 2018, Advance Article
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    Low-temperature FTIR spectroscopy provides evidence for protein-bound water molecules in eubacterial light-driven ion pumps

    Y. Nomura, S. Ito, M. Teranishi, H. Ono, K. Inoue and H. Kandori, Phys. Chem. Chem. Phys., 2018, Advance Article , DOI: 10.1039/C7CP05674E

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