Protein engineering of cytochrome c by semisynthesis: substitutions at glutamic acid 66

Details

Serval ID
serval:BIB_9D523CE30066
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Protein engineering of cytochrome c by semisynthesis: substitutions at glutamic acid 66
Journal
Protein Engineering
Author(s)
Wallace  C. J., Corthesy  B. E.
ISSN
0269-2139 (Print)
Publication state
Published
Issued date
11/1986
Volume
1
Number
1
Pages
23-7
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct-Nov
Abstract
We have used protein semisynthesis to prepare four analogues of horse cytochrome c, in which the glutamic acid residue at position 66 has been removed and replaced by norvaline, glutamine, lysine and, as a methodological control, glutamic acid. This residue is quite strongly conserved in mitochondrial cytochrome c, and forms part of a cluster of acidic residues that occurs in all cytochromes c but whose function is obscure. Comparative studies of the physical and biochemical properties of the analogues have now disclosed two specific roles for Glu66 in the protein. It contributes significantly to the stabilization of the active conformation of the protein, probably by salt bridge formation, and it appears to participate in the redox-state-dependent ATP-binding site of cytochrome c. Our results also support two general views of the role of surface charged residues in cytochrome c, namely that their disposition influences both redox potential, through the electrostatic field felt at the redox centre, and the kinetics of electron transfer, through the dipole moment they generate.
Keywords
Amino Acid Sequence Animals Cytochrome c Group/*chemical synthesis Glutamates Glutamic Acid Horses Molecular Sequence Data Protein Engineering Structure-Activity Relationship
Pubmed
Web of science
Create date
25/01/2008 14:53
Last modification date
20/08/2019 15:03
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