Jump to main content
Jump to site search

Issue 3, 2009
Previous Article Next Article

Photocurrent attenuation by a single polar-to-nonpolar point mutation of channelrhodopsin-2

Author affiliations

Abstract

Channelrhodopsin-2 (ChR2), one of the algal light-gated cation channel rhodopsins, contains five peculiar glutamic acid residues in the N-terminal region corresponding to the second to third transmembrane helices. Here we made systematic mutations of these polar amino acid residues of ChR2 into nonpolar alanine, and evaluated their photocurrent properties. Amongst them, the photocurrent generated by the E97A mutation, ChR2(E97A), was much smaller than expected from its expression. The ChR2(E97A) photocurrent was similar to wild-type ChR2 in the kinetic profiles, the reversal potential and the dependency to the light power density. Our results suggest that the residue E97 is one of the molecular determinants involved in the ion flux regulation.

Graphical abstract: Photocurrent attenuation by a single polar-to-nonpolar point mutation of channelrhodopsin-2

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 09 Sep 2008, accepted on 12 Jan 2009 and first published on 22 Jan 2009


Article type: Paper
DOI: 10.1039/B815762F
Citation: Photochem. Photobiol. Sci., 2009,8, 328-336
  •   Request permissions

    Photocurrent attenuation by a single polar-to-nonpolar point mutation of channelrhodopsin-2

    Y. Sugiyama, H. Wang, T. Hikima, M. Sato, J. Kuroda, T. Takahashi, T. Ishizuka and H. Yawo, Photochem. Photobiol. Sci., 2009, 8, 328
    DOI: 10.1039/B815762F

Search articles by author