New results about structure, function and regulation of the chloroplast ATP synthase (CF0CF1)
Author:
Publisher
Wiley
Subject
Cell Biology,Plant Science,Genetics,General Medicine,Physiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1034/j.1399-3054.1999.106120.x/fullpdf
Reference57 articles.
1. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria;Abrahams;Nature,1994
2. Electron microscopy and single molecule averaging of subunit-deficient F1-ATPases from Escherichia coli and spinach chloroplasts;Akey;EMBO J,1983
3. The F0 subunits of the Escherichia coli F0F1-ATP synthase are sufficient to form a functional proton pore;Aris;J Biol Chem,1985
4. Reactivation of the chloroplast CF1-ATPase beta subunit by trace amounts of the CF1 alpha subunit suggests a chaperonin-like activity for CF1 alpha;Avni;J Biol Chem,1991
5. Zero-length crosslinking between subunit Δ and I of the H+-translocating ATPase of chloroplasts;Beckers;Biochim Biophys Acta,1992
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