Literature DB >> 1834174

Ca2+ release from caged-Ca2+ alters the FTIR spectrum of sarcoplasmic reticulum.

R Buchet1, I Jona, A Martonosi.   

Abstract

Light-induced Ca2+ release from the Ca2+ complex of Nitr-5 altered the FTIR spectra of sarcoplasmic reticulum vesicles and purified Ca(2+)-ATPase preparations. The principal changes seen in difference spectra obtained after and before illumination in the presence of Nitr-5.Ca2+ consisted of an increase in absorbance at 1663 and 1676 cm-1 and a decrease in absorbance at 1653 cm-1. The light-induced changes in FTIR spectra were prevented by vanadate or EGTA, indicating that they were associated with the formation of Ca2E1 enzyme intermediate. Other light-induced changes in the FTIR spectra at 1600-1250 cm-1 were not clearly related to the sarcoplasmic reticulum, and were attributed to photolysis of Nitr-5. The difference absorbance bands are narrow, suggesting that they originate from changes in side chain vibrations, although some changes in secondary structures may also contribute.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 1834174     DOI: 10.1016/0005-2736(91)90126-s

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  6 in total

1.  Use of helper enzymes for ADP removal in infrared spectroscopic experiments: application to Ca2+-ATPase.

Authors:  Man Liu; Eeva-Liisa Karjalainen; Andreas Barth
Journal:  Biophys J       Date:  2005-02-24       Impact factor: 4.033

Review 2.  Fourier transform infrared (FTIR) spectroscopy.

Authors:  Catherine Berthomieu; Rainer Hienerwadel
Journal:  Photosynth Res       Date:  2009-06-10       Impact factor: 3.573

3.  A time-resolved Fourier transformed infrared difference spectroscopy study of the sarcoplasmic reticulum Ca(2+)-ATPase: kinetics of the high-affinity calcium binding at low temperature.

Authors:  A Troullier; K Gerwert; Y Dupont
Journal:  Biophys J       Date:  1996-12       Impact factor: 4.033

4.  Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations.

Authors:  Julia Andersson; Karin Hauser; Eeva-Liisa Karjalainen; Andreas Barth
Journal:  Biophys J       Date:  2007-09-21       Impact factor: 4.033

5.  ATP-Induced phosphorylation of the sarcoplasmic reticulum Ca2+ ATPase: molecular interpretation of infrared difference spectra.

Authors:  A Barth; W Mäntele
Journal:  Biophys J       Date:  1998-07       Impact factor: 4.033

6.  Side-chain protonation and mobility in the sarcoplasmic reticulum Ca2+-ATPase: implications for proton countertransport and Ca2+ release.

Authors:  K Hauser; A Barth
Journal:  Biophys J       Date:  2007-11-01       Impact factor: 4.033

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.