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Distances between the functional sites of sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase and the lipid/water interface.

作者信息

Teruel J A, Gómez-Fernández J C

出版信息

Biochim Biophys Acta. 1986 Dec 16;863(2):178-84. doi: 10.1016/0005-2736(86)90257-9.

Abstract

Measurements of fluorescence energy transfer have been performed to determine the distance between the lipid-water interface and the ATP-binding site in the (Ca2+ + Mg2+)-ATPase from sarcoplasmic reticulum. The calculated distance between the donor, FITC bound to the protein (nucleotide binding-site marker), and the acceptor, rhodamine-5'-isothiocyanyldipalmitoylphosphatidylethanolamine (RITC-DPPE) incorporated in the membrane, was in the range of 34-42 A. In addition the distance between the high affinity Ca2+-binding sites and the lipid/water interface has been calculated by luminescence energy transfer from Tb3+ bound to the Ca2+ sites to RITC-DPPE included in the membrane, and it was approx. 10 A.

摘要

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