Cytochrome c heme lyase can mature a fusion peptide composed of the amino-terminal residues of horse cytochrome c

2012 ◽  
Vol 48 (67) ◽  
pp. 8344 ◽  
Author(s):  
Wesley B. Asher ◽  
Kara L. Bren
Keyword(s):  
Cytochrome C ◽  
Fusion Peptide ◽  
Amino Terminal ◽  
Cytochrome C Heme Lyase ◽  
Horse Cytochrome

scholarly journals Role of cytochrome c heme lyase in the import of cytochrome c into mitochondria.

1988 ◽  
Vol 263 (35) ◽  
pp. 19034-19042 ◽  
Author(s):  
D W Nicholson ◽  
C Hergersberg ◽  
W Neupert
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Heme Lyase

scholarly journals The effect of complete or specific partial acetimidylation on the biological properties of cytochrome c and cytochrome c-T

1984 ◽  
Vol 217 (3) ◽  
pp. 595-599 ◽  
Author(s):  
C J A Wallace
Keyword(s):  
Structural Change ◽  
Cytochrome C ◽  
Oxygen Uptake ◽  
Redox Potential ◽  
Biological Properties ◽  
Amino Groups ◽  
Cytochromes C ◽  
Restricted Region ◽  
Horse Cytochrome

The biological consequences of acetimidylation of all 19 epsilon-amino groups of horse cytochrome c are a slight decrease in both the redox potential of the protein and its ability to stimulate oxygen uptake in the cytochrome c-depleted-mitochondria assay. Examination of a number of specific partially acetimidylated analogues and acetimidylated cytochromes c of other species has shown that the changes in biological properties, which are associated with a slight structural change as monitored by n.m.r. spectroscopy [Boswell, Moore, Williams, Harris, Wallace, Bocieck & Welti (1983) Biochem. J. 213, 679-686], appear to stem from modification of residues in a restricted region of the sequence. The failure of the redox potential of Saccharomyces cerevisae cytochrome c to be affected by acetimidylation suggests that it is lysine-53, absent from that species, that is the sensitive residue.

Analysis of the pH-dependent stability and millisecond folding kinetics of horse cytochrome c

2015 ◽  
Vol 585 ◽  
pp. 52-63 ◽  
Author(s):  
Rishu Jain ◽  
Rajesh Kumar ◽  
Sandeep Kumar ◽  
Ritika Chhabra ◽  
Mukesh Chand Agarwal ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Folding Kinetics ◽  
Ph Dependent ◽  
Kinetics Of ◽  
Horse Cytochrome

scholarly journals Effects of alterations of the amino-terminal glycine of influenza hemagglutinin fusion peptide on its structure, organization and membrane interactions

2003 ◽  
Vol 1612 (1) ◽  
pp. 41-51 ◽  
Author(s):  
Cheng-Wei Wu ◽  
Shu-Fang Cheng ◽  
Wei-Ning Huang ◽  
Vishwa Deo Trivedi ◽  
Balakrishnan Veeramuthu ◽  
...  
Keyword(s):  
Fusion Peptide ◽  
Membrane Interactions ◽  
Amino Terminal ◽  
Influenza Hemagglutinin
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