Fluorescence study on transmembrane Ca2+ gradient-mediated conformation changes of sarcoplasmic reticulum Ca2+-ATPase

Yaping Tu, F. Y. Yang

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The conformational states of Ca2+-ATPase in sarcoplasmic reticulum (SR) vesicles with or without a thousand-fold transmembrane Ca2+ gradient have been studied by fluorescence spectroscopy and fluorescence quenching. In consequence of the establishment of the transmembrane Ca2+ gradient, the steady-state fluorescence results revealed a reproducible 8% decrease in the intrinsic fluorescence while time-resolved fluorescence measurements showed that 13 tryptophan residues in SR · Ca2+-ATPase could be divided into three groups. The fluorescence lifetime of one of these groups increased from 5.5 ns to 5.95 ns in the presence of a Ca2+ gradient. Using KI and hypocrellin B (a photosensitive pigment obtained from a parasitic fungus, growing in Yunnan, China), the fluorescence quenching further indicated that the dynamic change of this tryptophan group, located at the protein-lipid interface, is a characteristic of transmembrane Ca2+ gradient-mediated conformational changes in SR · Ca2+-ATPase.

Original languageEnglish
Pages (from-to)309-317
Number of pages9
JournalBioscience Reports
Volume14
Issue number6
DOIs
StatePublished - Dec 1994
Externally publishedYes

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Calcium-Transporting ATPases
Sarcoplasmic Reticulum
Conformations
Fluorescence
Tryptophan
Quenching
Fluorescence Spectrometry
Fluorescence spectroscopy
Fungi
Pigments
China
Lipids
Proteins

All Science Journal Classification (ASJC) codes

  • Cell Biology
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Fluorescence study on transmembrane Ca2+ gradient-mediated conformation changes of sarcoplasmic reticulum Ca2+-ATPase. / Tu, Yaping; Yang, F. Y.

In: Bioscience Reports, Vol. 14, No. 6, 12.1994, p. 309-317.

Research output: Contribution to journalArticle

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