On the interaction between cytochrome f and plastocyanin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference10 articles.
1. ELECTRON TRANSFER IN ‘BLUE’ COPPER PROTEINS
2. X-ray crystal structure analysis of plastocyanin at 2.7 Å resolution
3. The effect of ethylenediamine chemical modification of plastocyanin on the rate of cytochrome f oxidation and P-700+ reduction
4. Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. 11. Effects of pH, competitive inhibition, and chromium(III) modification on the reaction of plastocyanin with cytochrome f
5. Nucleotide sequence of the gene for pre-apocytochrome f in the spinach plastid chromosome
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1. Surface interactions in the complex between cytochrome f and the E43Q/D44N and E59K/E60Q plastocyanin double mutants as determined by 1H-NMR chemical shift analysis;Protein Science;2008-12-31
2. Reduction of plastocyanin by tyrosine-containing oligopeptides;Journal of Inorganic Biochemistry;2006-11
3. Interaction of plastocyanin with oligopeptides: effect of lysine distribution within the peptide;Journal of Inorganic Biochemistry;2004-05
4. Surface interactions in the complex between cytochrome f and the E43Q/D44N and E59K/E60Q plastocyanin double mutants as determined by 1H-NMR chemical shift analysis;Protein Science;2001-11-19
5. Spectroscopic and Electrochemical Studies on Structural Change of Plastocyanin and Its Tyrosine 83 Mutants Induced by Interaction with Lysine Peptides;Biochemistry;2000-05-01
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