Structural changes underlying proton pumping by Bacteriorhodopsin

R. Henderson, P. Bullough, M. Lindahl, S. Subramaniam

Research output: Contribution to journalArticle

Abstract

Protons are released from the extracellular surface and subsequently taken up from the cytoplasmic side of the bacteriorhodopsin molecule during its photocycle. A number of spectroscopically distinct intermediates have been characterised by a wide variety of techniques. The structure of most of these intermediates can be examined directly by electron diffraction of two-dimensional crystals provided the intermediate can be trapped by rapidly freezing the specimens to liquid nitrogen temperature. In addition, a variety of mutant bacteriorhodopsin molecules have perturbed photocycles which provide additional opportunities to examine the behaviour of the structure following a light flash. Proton release on the extracellular side and cytoplasmic uptake require opposite vectoriality in the Schiff base accessibility. The nature and size of the structure change required to provide this vectorial change in accessibility, the "gating" of the channels, will be described.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number9
StatePublished - 1997
Externally publishedYes

Fingerprint

Bacteriorhodopsins
protons
Protons
Molecules
Schiff Bases
Liquid nitrogen
Freezing
Electron diffraction
crystals
freezing
Nitrogen
electrons
Electrons
Light
mutants
Crystals
Temperature
liquids
nitrogen
temperature

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Henderson, R., Bullough, P., Lindahl, M., & Subramaniam, S. (1997). Structural changes underlying proton pumping by Bacteriorhodopsin. FASEB Journal, 11(9).

Structural changes underlying proton pumping by Bacteriorhodopsin. / Henderson, R.; Bullough, P.; Lindahl, M.; Subramaniam, S.

In: FASEB Journal, Vol. 11, No. 9, 1997.

Research output: Contribution to journalArticle

Henderson, R, Bullough, P, Lindahl, M & Subramaniam, S 1997, 'Structural changes underlying proton pumping by Bacteriorhodopsin', FASEB Journal, vol. 11, no. 9.
Henderson R, Bullough P, Lindahl M, Subramaniam S. Structural changes underlying proton pumping by Bacteriorhodopsin. FASEB Journal. 1997;11(9).
Henderson, R. ; Bullough, P. ; Lindahl, M. ; Subramaniam, S. / Structural changes underlying proton pumping by Bacteriorhodopsin. In: FASEB Journal. 1997 ; Vol. 11, No. 9.
@article{fbf76b6ae05f4424bb1386c889fabff7,
title = "Structural changes underlying proton pumping by Bacteriorhodopsin",
abstract = "Protons are released from the extracellular surface and subsequently taken up from the cytoplasmic side of the bacteriorhodopsin molecule during its photocycle. A number of spectroscopically distinct intermediates have been characterised by a wide variety of techniques. The structure of most of these intermediates can be examined directly by electron diffraction of two-dimensional crystals provided the intermediate can be trapped by rapidly freezing the specimens to liquid nitrogen temperature. In addition, a variety of mutant bacteriorhodopsin molecules have perturbed photocycles which provide additional opportunities to examine the behaviour of the structure following a light flash. Proton release on the extracellular side and cytoplasmic uptake require opposite vectoriality in the Schiff base accessibility. The nature and size of the structure change required to provide this vectorial change in accessibility, the {"}gating{"} of the channels, will be described.",
author = "R. Henderson and P. Bullough and M. Lindahl and S. Subramaniam",
year = "1997",
language = "English (US)",
volume = "11",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "9",

}

TY - JOUR

T1 - Structural changes underlying proton pumping by Bacteriorhodopsin

AU - Henderson, R.

AU - Bullough, P.

AU - Lindahl, M.

AU - Subramaniam, S.

PY - 1997

Y1 - 1997

N2 - Protons are released from the extracellular surface and subsequently taken up from the cytoplasmic side of the bacteriorhodopsin molecule during its photocycle. A number of spectroscopically distinct intermediates have been characterised by a wide variety of techniques. The structure of most of these intermediates can be examined directly by electron diffraction of two-dimensional crystals provided the intermediate can be trapped by rapidly freezing the specimens to liquid nitrogen temperature. In addition, a variety of mutant bacteriorhodopsin molecules have perturbed photocycles which provide additional opportunities to examine the behaviour of the structure following a light flash. Proton release on the extracellular side and cytoplasmic uptake require opposite vectoriality in the Schiff base accessibility. The nature and size of the structure change required to provide this vectorial change in accessibility, the "gating" of the channels, will be described.

AB - Protons are released from the extracellular surface and subsequently taken up from the cytoplasmic side of the bacteriorhodopsin molecule during its photocycle. A number of spectroscopically distinct intermediates have been characterised by a wide variety of techniques. The structure of most of these intermediates can be examined directly by electron diffraction of two-dimensional crystals provided the intermediate can be trapped by rapidly freezing the specimens to liquid nitrogen temperature. In addition, a variety of mutant bacteriorhodopsin molecules have perturbed photocycles which provide additional opportunities to examine the behaviour of the structure following a light flash. Proton release on the extracellular side and cytoplasmic uptake require opposite vectoriality in the Schiff base accessibility. The nature and size of the structure change required to provide this vectorial change in accessibility, the "gating" of the channels, will be described.

UR - http://www.scopus.com/inward/record.url?scp=33750099380&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750099380&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33750099380

VL - 11

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 9

ER -