help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Barth, A.
Right arrow Articles by Corrie, J. E. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Barth, A.
Right arrow Articles by Corrie, J. E. T.

Biophys J, November 2002, p. 2864-2871, Vol. 83, No. 5

Characterization of a New Caged Proton Capable of Inducing Large pH Jumps

Andreas Barth* and John E. T. Corriedagger

 *Institut für Biophysik, Johann Wolfgang Goethe-Universität, D-60590 Frankfurt am Main, Germany, and  dagger National Institute for Medical Research, London NW7 1AA, United Kingdom

A new caged proton, 1-(2-nitrophenyl)ethyl sulfate (caged sulfate), is characterized by infrared spectroscopy and compared with a known caged, proton 2-hydroxyphenyl 1-(2-nitrophenyl)ethyl phosphate (caged HPP). In contrast to caged HPP, caged sulfate can induce large pH jumps and protonate groups that have pK values as low as 2.2. The photolysis mechanism of caged sulfate is analogous to that of P3-[1-(2-nitrophenyl)ethyl] ATP (caged ATP), and the photolysis efficiency is similar. The utility of this new caged compound for biological studies was demonstrated by its ability to drive the acid-induced conformational change of metmyoglobin. This transition from the native conformation to a partially unfolded form takes place near pH 4 and was monitored by near-UV absorption spectroscopy.

Biophys J, November 2002, p. 2864-2871, Vol. 83, No. 5
© 2002 by the Biophysical Society   0006-3495/02/11/2864/08  $2.00


This article has been cited by other articles:


Home page
 FASEB J.Home page
D. Basting, M. Lorch, I. Lehner, and C. Glaubitz
Transport cycle intermediate in small multidrug resistance protein is revealed by substrate fluorescence
FASEB J, February 1, 2008; 22(2): 365 - 373.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. Fibich, K. Janko, and H.-J. Apell
Kinetics of Proton Binding to the Sarcoplasmic Reticulum Ca-ATPase in the E1 State
Biophys. J., November 1, 2007; 93(9): 3092 - 3104.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
C. J. Kastrup, M. K. Runyon, F. Shen, and R. F. Ismagilov
From the Cover: Modular chemical mechanism predicts spatiotemporal dynamics of initiation in the complex network of hemostasis
PNAS, October 24, 2006; 103(43): 15747 - 15752.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Biophysical Society.