0000000000555917
AUTHOR
J. Heidemeier
Investigation of the dynamics of bacteriorhodopsin
Bacteriorhodopsin (bR) converted to the blue form by deionization has been reconstituted to the active purple membrane by addition of57Fe ions. Mossbauer spectra measured in a wide temperature range reveal Fe3+ binding places with oxygen atoms in the neighbourhood. No evidence for a well defined functional binding place of the iron has been found. On a timescale faster 100 ns the purple membrane shows increasing flexibility above 200 K. In order to analyse the influence of the lipids, a bacteriorhodopsin sample where the lipid content has been increased artificially by the incorporation of DMPC as well as a sample consisting of lipid bilayer have been investigated.
The photocycle and the structure of iron containing bacteriorhodopsin ?a kinetic and M�ssbauer spectroscopy investigation
Bacteriorhodopsin (bR), converted by deionization to the blue form was reconstituted to the active purple membrane by the addition of Fe2+ or Fe3+ ions. 57Fe Mossbauer spectra of these samples were measured at different pH values (pH 3.9, pH 5.0 and pH 7.0) and at temperatures ranging from 4 K to 300 K. The hyperfine parameters reveal two iron environments with oxygen atoms in the neighbourhood of iron. Iron type 1 is in the 3+ high spin state. It is bound to acid side chains of the protein and/or the phosphate groups of the lipids. Iron type 2 is in the 2+ high spin state and is linked to carboxy groups of the protein in a rather unspecific way. Dynamics as measured by Mossbauer spectrosco…