The Structure of the Heme Crevice of Ferric Cytochrome c Alkylated at Methionine-80
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference13 articles.
1. The 695-mμ Band of Ferricytochrome c and Its Relationship to Protein Conformation*
2. Modification of the tryptophanyl residue of horse heart cytochrome
3. Reaction of cytochrome c with imidazole
4. The Effects of Alkylation of Methionyl Residues on the Properties of Horse Cytochrome c
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1. Peroxynitrite detoxification by horse heart carboxymethylated cytochrome c is allosterically modulated by cardiolipin;Biochemical and Biophysical Research Communications;2011-11
2. Relationship between local and global stabilities of proteins: site-directed mutants and chemically-modified derivatives of cytochrome c;Biochemistry;1992-09-01
3. Ligand binding to cytochrome c and other related haem proteins and peptides. Part I. Equilibrium studies;Inorganica Chimica Acta;1988-10
4. Reduction of horse heart ferricytochrome c by glutathione: Evidence for two different conformational forms of ferricytochrome c in neutral and slightly alkaline solutions;Biochemical and Biophysical Research Communications;1978-06
5. The role of lysines in Euglena cytochrome c-552;Archives of Biochemistry and Biophysics;1977-05
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