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Structural Dynamics of Light-Driven Proton Pumps

Andersson, Magnus (author)
Chalmers tekniska högskola,Chalmers University of Technology
Malmerberg, Erik, 1980 (author)
Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry
Westenhoff, Sebastian, 1978 (author)
Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry
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Katona, Gergely, 1975 (author)
Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry
Cammarata, Marco (author)
European Synchrotron Radiation Facility (ESRF)
Wöhri, Annemarie, 1976 (author)
Chalmers tekniska högskola,Chalmers University of Technology
Johansson, Linda C, 1983 (author)
Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry
Ewald, Friederike (author)
European Synchrotron Radiation Facility (ESRF)
Eklund, Mattias (author)
Uppsala universitet,Institutionen för fotokemi och molekylärvetenskap,Uppsala University
Wulff, Michael (author)
European Synchrotron Radiation Facility (ESRF)
Davidsson, Jan (author)
Uppsala universitet,Institutionen för fotokemi och molekylärvetenskap,Uppsala University
Neutze, Richard, 1969 (author)
Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry
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 (creator_code:org_t)
Elsevier BV, 2009
2009
English.
In: Structure. - : Elsevier BV. - 0969-2126 .- 1878-4186. ; 17:9, s. 1265-1275
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Bacteriorhodopsin and proteorhodopsin are simple heptahelical proton pumps containing a retinal chromophore covalently bound to helix G via a protonated Schiff base. Following the absorption of a photon, all-trans retinal is isomerized to a 13-cis conformation, initiating a sequence of conformational changes driving vectorial proton transport. In this study we apply time-resolved wide-angle X-ray scattering to visualize in real time the helical motions associated with proton pumping by bacteriorhodopsin and proteorhodopsin. Our results establish that three conformational states are required to describe their photocycles. Significant motions of the cytoplasmic half of helix F and the extracellular half of helix C are observed prior to the primary proton transfer event, which increase in amplitude following proton transfer. These results both simplify the structural description to emerge from intermediate trapping studies of bacteriorhodopsin and reveal shared dynamical principles for proton pumping.

Subject headings

NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

Keyword

Chemistry
Kemi

Publication and Content Type

ref (subject category)
art (subject category)

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