On the specificity of cytochrome c synthetase in recognition of the amino acid sequence of apocytochrome c.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
1. Formation of an iso-1-cytochrome c-like species containing a covalently bonded heme group from the apoprotein by a yeast cell-free system in the presence of hemin.
2. Formation of a cytochrome c-like species from horse apoprotein and hemin catalyzed by yeast mitochondrial cytochrome c synthetase.
3. Evidence for formation of two thioether bonds to link heme to apocytochrome c by partially purified cytochrome c synthetase.
4. Assembly of Cytochrome c. Apocytochrome c Is Bound to Specific Sites on Mitochondria before Its Conversion to Holocytochrome c
5. Synthesis of a heme fragment of horse cytochrome c which forms a productive complex with a native apofragment.
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1. Mechanisms of Mitochondrial Holocytochrome c Synthase and the Key Roles Played by Cysteines and Histidine of the Heme Attachment Site, Cys-XX-Cys-His;Journal of Biological Chemistry;2014-10
2. Conserved Residues of the Human Mitochondrial Holocytochrome c Synthase Mediate Interactions with Heme;Biochemistry;2014-08-06
3. Cytochrome c biogenesis in mitochondria - Systems III and V;FEBS Journal;2011-08-02
4. Complexation which facilitates rejoining of horse cytochrome c apofragment [Homoser-lactone65](1-65) or [Homoser-lactone65] (23-65) to apofragment (66-104);International Journal of Peptide and Protein Research;2009-01-12
5. Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes;Advances in Microbial Physiology;2002
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