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Biophysical Journal 70: 852-856 (1996)
© 1996 the Biophysical Society

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An extended x-ray absorption fine structure study of the high-affinity cation-binding site in the purple membrane.

F Sepulcre, J Cladera, J García, M G Proietti, J Torres and E Padrós

Department de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Spain.

ABSTRACT

The structure of the high-affinity cation-binding site of bacteriorhodopsin was studied using extended x-ray absorption fine structure techniques. The results obtained for Mn2+ in aqueous solution and for the complex BR-Mn2+ (1:1 molar ratio) show great similarities, suggesting that Mn2+, when bound to this site, is coordinated with six atoms of oxygen, forming an octahedral disposition. The interatomic distance between the atoms of oxygen and the Mn2+ was found to be 2.17 A for the complex BR-Mn2+, similar to Mn2+ in solution (2.15 A). In addition, the absence of any other peak at greater distances in the Fourier-transformed spectrum indicates that neither phosphorus nor sulphur atoms are present in the second coordination shell. This suggests that this binding site is located in the protein, discarding the proximity of lipid polar headgroups.




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F. Sepulcre, M. G. Proietti, M. Benfatto, S. Della Longa, J. Garcia, and E. Padros
A Quantitative XANES Analysis of the Calcium High-Affinity Binding Site of the Purple Membrane
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[Abstract] [Full Text] [PDF]

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C. Sanz, M. Marquez, A. Peralvarez, S. Elouatik, F. Sepulcre, E. Querol, T. Lazarova, and E. Padros
Contribution of Extracellular Glu Residues to the Structure and Function of Bacteriorhodopsin. PRESENCE OF SPECIFIC CATION-BINDING SITES
J. Biol. Chem., October 26, 2001; 276(44): 40788 - 40794.
[Abstract] [Full Text] [PDF]


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Copyright © 1996 by the Biophysical Society.