Match!

Long-distance perturbation on Schiff base–counterion interactions by His30 and the extracellular Na+-binding site in Krokinobacter rhodopsin 2

Published on Jan 1, 2018in Physical Chemistry Chemical Physics3.57
· DOI :10.1039/C8CP00626A
Arisu Shigeta3
Estimated H-index: 3
(Yokohama National University),
Shota Ito7
Estimated H-index: 7
(Nagoya Institute of Technology)
+ 4 AuthorsIzuru Kawamura14
Estimated H-index: 14
(Yokohama National University)
Abstract
Krokinobacter rhodopsin 2 (KR2), a light-driven Na+ pump, is a dual-functional protein, pumping protons in the absence of Na+ when K+ or larger alkali metal ions are present. A specific mutation in helix A near the extracellular Na+ binding site, H30A, eliminates its proton pumping ability. We induced structural changes in H30A by altering the alkali metal ion bound at the extracellular binding site, and observed a strong electrostatic interaction between the Schiff base and counterion and torsion around the Schiff base as revealed by solid-state nuclear magnetic resonance (NMR) and Fourier transform infrared (FTIR) spectroscopies. The strong interaction when His30 was absent and no ion bound at the extracellular binding site disabled retinal reisomerization, as was shown with flash-photolysis, forming a small amount of only a K-like intermediate. This revealed why H30A lacks the proton pumping function. Long-distance perturbation of the binding site and Schiff base revealed that a non-transported ion binding at the extracellular site is essential for pumping.
  • References (29)
  • Citations (2)
References29
Newest
#1Hongshen Zhao (CAS: Chinese Academy of Sciences)H-Index: 1
#2Baofu Ma (CAS: Chinese Academy of Sciences)H-Index: 1
Last.CHENDeliang (CAS: Chinese Academy of Sciences)H-Index: 9
view all 6 authors...
5 CitationsSource
#1Akiko Niho (Okayama University)H-Index: 1
#2Susumu Yoshizawa (UTokyo: University of Tokyo)H-Index: 12
Last.Yuki SudoH-Index: 27
view all 11 authors...
9 CitationsSource
#1Arisu ShigetaH-Index: 3
#2Shota ItoH-Index: 7
Last.Izuru KawamuraH-Index: 14
view all 7 authors...
7 CitationsSource
#1Hideaki E. Kato (Stanford University)H-Index: 16
#2Keiichi Inoue (Nagoya Institute of Technology)H-Index: 21
Last.Osamu Nureki (UTokyo: University of Tokyo)H-Index: 56
view all 4 authors...
6 CitationsSource
#1I. Gushchin (MIPT: Moscow Institute of Physics and Technology)H-Index: 10
#2Vitaly Shevchenko (MIPT: Moscow Institute of Physics and Technology)H-Index: 6
Last.Valentin I. GordeliyH-Index: 23
view all 7 authors...
10 CitationsSource
13 CitationsSource
#1Yusaku Hontani (VU: VU University Amsterdam)H-Index: 7
#2Keiichi Inoue (Nagoya Institute of Technology)H-Index: 21
Last.John T. M. Kennis (VU: VU University Amsterdam)H-Index: 38
view all 6 authors...
10 CitationsSource
12 CitationsSource
#1I. GushchinH-Index: 10
#2Vitaly Shevchenko (MIPT: Moscow Institute of Physics and Technology)H-Index: 6
Last.Valentin I. GordeliyH-Index: 23
view all 16 authors...
66 CitationsSource
#1Hideaki E. KatoH-Index: 16
#2Keiichi InoueH-Index: 21
Last.Osamu NurekiH-Index: 56
view all 23 authors...
80 CitationsSource
Cited By2
Newest
#1K. KovalevH-Index: 5
#2Vitaly Polovinkin (CNRS: Centre national de la recherche scientifique)H-Index: 1
Last.Valentin I. Gordeliy (MIPT: Moscow Institute of Physics and Technology)H-Index: 23
view all 15 authors...
4 CitationsSource
#1Jagdeep Kaur (Goethe University Frankfurt)H-Index: 3
#2Clara Nassrin Kriebel (Goethe University Frankfurt)H-Index: 1
Last.Clemens Glaubitz (Goethe University Frankfurt)H-Index: 32
view all 12 authors...
5 CitationsSource
View next paperCalcium binding to the purple membrane: A molecular dynamics study