Document Detail

Role of lysines in the cytochrome c - cardiolipin interaction.
MedLine Citation:
PMID:  23738909     Owner:  NLM     Status:  Publisher    
Cytochrome c undergoes structural variations during the apoptotic process; such changes have been related with modifications occurring in the protein when it forms a complex with cardiolipin, one of the phospholipids constituting the mitochondrial membrane. Although several studies have been performed to identify the site(s) of the protein involved in the cytochrome c/cardiolipin interaction, to date the location of this hosting region(s) remains unidentified and is a matter of debate. To gain a deeper insight into the reaction mechanism, we investigate the role that the Lys72, Lys73 and Lys79 residues play in the cytochrome c/cardiolipin interaction, as these side chains appear to be critical for cytochrome c/cardiolipin recognition. The Lys72Asn, Lys73Asn, Lys79Asn, Lys72/73Asn and Lys72/73/79Asn mutants of horse heart cytochrome c were produced and characterized by circular dichroism, UV-visible and resonance Raman spectroscopies, and the effects of the mutations on the interaction of the variants with cardiolipin have been investigated. The mutants are characterized by a subpopulation with non-native axial coordination, and are less stable than the wild type protein. Furthermore, the mutants lacking Lys72 and/or Lys79 do not bind cardiolipin and those lacking Lys73, although they form a complex with the phospholipid, do not show any peroxidase activity. These observations indicate that the Lys72, Lys73 and Lys79 residues stabilize the native axial Met80-Fe(III) coordination as well as the tertiary structure of cytochrome c. Moreover, while Lys72 and Lys79 are critical for cytochrome c/cardiolipin recognition, the simultaneous presence of Lys72, Lys73 and Lys79 is necessary for peroxidase activity of cardiolipin-bound cytochrome c.
Federica Sinibaldi; Barry D Howes; Enrica Droghetti; Fabio Polticelli; Maria Cristina Piro; Donato Di Pierro; Laura Fiorucci; Massimo Coletta; Giulietta Smulevich; Roberto Santucci
Related Documents :
23149229 - 6,7-dihydroxy-1-oxoisoindoline-4-sulfonamide-containing hiv-1 integrase inhibitors.
24682739 - Probing for improved potency and in vivo bioavailability of excitatory amino acid trans...
24900769 - Identification of ml251, a potent inhibitor of t. brucei and t. cruzi phosphofructokinase.
24697269 - Development of pyrazolone and isoxazol-5-one cambinol analogs as sirtuin inhibitors.
20205649 - Salt effect on substrate specificity of a subtilisin-like halophilic protease.
16959319 - Enzymatic and spectroscopic studies on the activation or inhibition effects by substitu...
8646539 - Crystal structure of the escherichia coli dutpase in complex with a substrate analogue ...
24197829 - Residues of endosulfan in carp as an indicator of exposure conditions.
7760939 - Structure of tubulin at 6.5 a and location of the taxol-binding site.
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-6-5
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2013 Jun 
Date Detail:
Created Date:  2013-6-6     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Lidocaine-prilocaine (EMLA(®) ) cream as analgesia in hysteroscopy practice: a prospective, randomiz...
Next Document:  Evaluation of insulin initiation on resource utilization and direct costs of treatment over 12 month...