Interaction of cytochrome c with the blue copper proteins, plastocyanin and azurin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
1. An enzyme kinetics and fluorine-19 nuclear magnetic resonance study of selectively trifluoroacetylated cytochrome c derivatives
2. Effect of specific trifluoroacetylation of individual cytochrome c lysines on the reaction with cytochrome oxidase
3. Use of specific lysine modifications to locate the reaction site of cytochrome c with cytochrome oxidase
4. Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5
5. Definition of cytochrome c binding domains by chemical modification. III. Kinetics of reaction of carboxydinitrophenyl cytochromes c with cytochrome c oxidase.
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1. Motion of redox molecules in solution monitored by the highly-sensitive EQCM technique;Research on Chemical Intermediates;2006-03
2. Direct electrochemistry of blue copper proteins at boron-doped diamond electrodes;Electrochimica Acta;2005-05
3. Direct monitoring of the electron pool effect of cytochrome c3 by highly sensitive EQCM measurements;JBIC Journal of Biological Inorganic Chemistry;2004-10-28
4. Metalloprotein Association, Self-Association, and Dynamics Governed by Hydrophobic Interactions: Simultaneous Occurrence of Gated and True Electron-Transfer Reactions between Cytochrome f and Cytochrome c6 from Chlamydomonas reinhardtii;Journal of the American Chemical Society;2003-08-08
5. From the protein–polypeptide model system to the interaction between physiological partners using electrochemistry;Journal of Electroanalytical Chemistry;2002-04
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