Detection of a Yb3+ Binding Site in Regenerated Bacteriorhodopsin That is Coordinated with the Protein and Phospholipid Head Groups

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1996 Dec 10

PMID 8962051

Citations 3

Authors

C Roselli

A Boussac

T A Mattioli

J A Griffiths

M A El-Sayed

Affiliations

Soon will be listed here.

Abstract

Near infrared Yb3+ vibronic sideband spectroscopy was used to characterize specific lanthanide binding sites in bacteriorhodopsin (bR) and retinal free bacteriorhodopsin (bO). The VSB spectra for deionized bO regenerated with a ratio of 1:1 and 2:1 ion to bO are identical. Application of a two-dimensional anti-correlation technique suggests that only a single Yb3+ site is observed. The Yb3+ binding site in bO is observed to consist of PO2- groups and carboxylic acid groups, both of which are bound in a bidentate manner. An additional contribution most likely arising from a phenolic group is also observed. This implies that the ligands for the observed single binding site are the lipid head groups and amino acid residues. The vibronic sidebands of Yb3+ in deionized bR regenerated at a ratio of 2:1 ion to bR are essentially identical to those in bO. The other high-affinity binding site is thus either not evident or its fluorescence is quenched. A discussion is given on the difference in binding of Ca2+ (or Mg2+) and lanthanides in phospholipid membrane proteins.

Citing Articles

Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMR.

TUZI S, Yamaguchi S, Tanio M, Konishi H, Inoue S, Naito A Biophys J. 1999; 76(3):1523-31.

PMID: 10049332 PMC: 1300128. DOI: 10.1016/S0006-3495(99)77311-X.

Experimental and theoretical characterization of the high-affinity cation-binding site of the purple membrane.

Pardo L, Sepulcre F, Cladera J, Dunach M, Labarta A, Tejada J Biophys J. 1998; 75(2):777-84.

PMID: 9675179 PMC: 1299752. DOI: 10.1016/S0006-3495(98)77567-8.

Studies of cation binding in ZnCl2-regenerated bacteriorhodopsin by x-ray absorption fine structures: effects of removing water molecules and adding Cl- ions.

Zhang K, Song L, Dong J, El-Sayed M Biophys J. 1997; 73(4):2097-105.

PMID: 9336205 PMC: 1181110. DOI: 10.1016/S0006-3495(97)78240-7.

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