Functional roles of tyrosine 185 during the bacteriorhodopsin photocycle as revealed by in situ spectroscopic studies

Xiaoyan Ding, Chao Sun, Haolin Cui, Sijin Chen, Yujiao Gao, Yanan Yang, Juan Wang, Xiao He, Dinu Iuga, Fang Tian, Anthony Watts, Xin Zhao

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Tyrosine 185 (Y185), one of the aromatic residues within the retinal (Ret) chromophore binding pocket in helix F of bacteriorhodopsin (bR), is highly conserved among the microbial rhodopsin family proteins. Many studies have investigated the functions of Y185, but its underlying mechanism during the bR photocycle remains unclear. To address this research gap, in situ two-dimensional (2D) magic-angle spinning (MAS) solid-state NMR (ssNMR) of specifically labelled bR, combined with light-induced transient absorption change measurements, dynamic light scattering (DLS) measurements, titration analysis and site-directed mutagenesis, was used to elucidate the functional roles of Y185 during the bR photocycle in the native membrane environment. Different interaction modes were identified between Y185 and the Ret chromophore in the dark-adapted (inactive) state and M (active) state, indicating that Y185 may serve as a rotamer switch maintaining the protein dynamics, and plays an important role in the efficient proton-pumping mechanism in the bR purple membrane.

Original languageEnglish (US)
Pages (from-to)1006-1014
Number of pages9
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1859
Issue number10
DOIs
StatePublished - Oct 1 2018

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Bacteriorhodopsins
Tyrosine
Chromophores
Microbial Rhodopsins
Purple Membrane
Membranes
Mutagenesis
Magic angle spinning
Dynamic light scattering
Site-Directed Mutagenesis
Titration
Protons
Proteins
Switches
Nuclear magnetic resonance
Light
Research

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

Ding, Xiaoyan ; Sun, Chao ; Cui, Haolin ; Chen, Sijin ; Gao, Yujiao ; Yang, Yanan ; Wang, Juan ; He, Xiao ; Iuga, Dinu ; Tian, Fang ; Watts, Anthony ; Zhao, Xin. / Functional roles of tyrosine 185 during the bacteriorhodopsin photocycle as revealed by in situ spectroscopic studies. In: Biochimica et Biophysica Acta - Bioenergetics. 2018 ; Vol. 1859, No. 10. pp. 1006-1014.
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abstract = "Tyrosine 185 (Y185), one of the aromatic residues within the retinal (Ret) chromophore binding pocket in helix F of bacteriorhodopsin (bR), is highly conserved among the microbial rhodopsin family proteins. Many studies have investigated the functions of Y185, but its underlying mechanism during the bR photocycle remains unclear. To address this research gap, in situ two-dimensional (2D) magic-angle spinning (MAS) solid-state NMR (ssNMR) of specifically labelled bR, combined with light-induced transient absorption change measurements, dynamic light scattering (DLS) measurements, titration analysis and site-directed mutagenesis, was used to elucidate the functional roles of Y185 during the bR photocycle in the native membrane environment. Different interaction modes were identified between Y185 and the Ret chromophore in the dark-adapted (inactive) state and M (active) state, indicating that Y185 may serve as a rotamer switch maintaining the protein dynamics, and plays an important role in the efficient proton-pumping mechanism in the bR purple membrane.",
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Functional roles of tyrosine 185 during the bacteriorhodopsin photocycle as revealed by in situ spectroscopic studies. / Ding, Xiaoyan; Sun, Chao; Cui, Haolin; Chen, Sijin; Gao, Yujiao; Yang, Yanan; Wang, Juan; He, Xiao; Iuga, Dinu; Tian, Fang; Watts, Anthony; Zhao, Xin.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1859, No. 10, 01.10.2018, p. 1006-1014.

Research output: Contribution to journalArticle

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T1 - Functional roles of tyrosine 185 during the bacteriorhodopsin photocycle as revealed by in situ spectroscopic studies

AU - Ding, Xiaoyan

AU - Sun, Chao

AU - Cui, Haolin

AU - Chen, Sijin

AU - Gao, Yujiao

AU - Yang, Yanan

AU - Wang, Juan

AU - He, Xiao

AU - Iuga, Dinu

AU - Tian, Fang

AU - Watts, Anthony

AU - Zhao, Xin

PY - 2018/10/1

Y1 - 2018/10/1

N2 - Tyrosine 185 (Y185), one of the aromatic residues within the retinal (Ret) chromophore binding pocket in helix F of bacteriorhodopsin (bR), is highly conserved among the microbial rhodopsin family proteins. Many studies have investigated the functions of Y185, but its underlying mechanism during the bR photocycle remains unclear. To address this research gap, in situ two-dimensional (2D) magic-angle spinning (MAS) solid-state NMR (ssNMR) of specifically labelled bR, combined with light-induced transient absorption change measurements, dynamic light scattering (DLS) measurements, titration analysis and site-directed mutagenesis, was used to elucidate the functional roles of Y185 during the bR photocycle in the native membrane environment. Different interaction modes were identified between Y185 and the Ret chromophore in the dark-adapted (inactive) state and M (active) state, indicating that Y185 may serve as a rotamer switch maintaining the protein dynamics, and plays an important role in the efficient proton-pumping mechanism in the bR purple membrane.

AB - Tyrosine 185 (Y185), one of the aromatic residues within the retinal (Ret) chromophore binding pocket in helix F of bacteriorhodopsin (bR), is highly conserved among the microbial rhodopsin family proteins. Many studies have investigated the functions of Y185, but its underlying mechanism during the bR photocycle remains unclear. To address this research gap, in situ two-dimensional (2D) magic-angle spinning (MAS) solid-state NMR (ssNMR) of specifically labelled bR, combined with light-induced transient absorption change measurements, dynamic light scattering (DLS) measurements, titration analysis and site-directed mutagenesis, was used to elucidate the functional roles of Y185 during the bR photocycle in the native membrane environment. Different interaction modes were identified between Y185 and the Ret chromophore in the dark-adapted (inactive) state and M (active) state, indicating that Y185 may serve as a rotamer switch maintaining the protein dynamics, and plays an important role in the efficient proton-pumping mechanism in the bR purple membrane.

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