Rei Abe-Yoshizumi

TL;DR: It is discovered that the marine flavobacterium Krokinobacter eikastus possesses two rhodopsins, the first, KR1, being a prototypical proton pump, while the second, KR2, pumps sodium ions outward.

TL;DR: Crystal structures of KR2 under neutral and acidic conditions are presented, which represent the resting and M-like intermediate states, respectively, and reveal the molecular basis for light-driven non-proton cation pumps and provide a framework that may advance the development of next-generation optogenetics.

TL;DR: High-speed atomic force microscopy is used to directly observe the oligomeric states in the lipid membrane of various microbial rhodopsins found within eubacteria to archaea, demonstrating that the stoichiometry of the fundamental oligomer of microbial r Rhodopsins strongly correlate with the phylogenetic tree.

TL;DR: The 2.4-Å-resolution structure of HeR from an uncultured Thermoplasmatales archaeon SG8-52-1 shows that it adopts a similar fold to that of type I rhodopsin—despite the low sequence identity—but there are also several marked differences that provide insights into heliorhodopin function.

TL;DR: In this paper, the authors applied light-induced difference Fourier transform infrared (FTIR) spectroscopy to a compatible sodium ion-proton pump, at 77 K, and found that the structure and structural changes in the primary processes of KR2 are common to all microbial rhodopsins.