Photoaffinity cross-linking of F1ATPase from spinach chloroplasts by 3'-arylazido-β-alanyl-8-azido ATP
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)80151-7/fullpdf
Reference51 articles.
1. The Mr -value of chloroplast coupling factor 1
2. Structure, Function, and Regulation of Chloroplast ATPase
3. P. Gräber B. Böttcher E.J. Boekema G. Milazzo M. Blank Bioelectrochemistry III 1990 Plenum Press New York 247 276
4. G.B. Cox R.J. Devenish F. Gibson S.M. Howitt P. Nagley L. Ernster Molecular Mechanisms in Bioenergetics 1992 283 315
5. Chloroplast F1 ATPase has more than three nucleotide binding sites, and 2-azido-ADP or 2-azido-ATP at both catalytic and noncatalytic sites labels the .beta. subunit
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1. Nitrenium Ions and Related Species in Photoaffinity Labeling;Nitrenes and Nitrenium Ions;2013-04-09
2. The Low-Affinity ATP Binding Site of the Escherichia coli SecA Dimer Is Localized at the Subunit Interface;Biochemistry;1997-12-01
3. 2,8-Diazido-ATP - a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1in ATP synthase (from thermophilic bacteria PS3);FEBS Letters;1995-12-27
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