Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin

We report a resonance Raman and UV-vis characterization of the active site structure of oxidatively modified forms of cytochrome c (Cyt-c) free in solution and in complexes with cardiolipin (CL). The studied post-translational modifications of Cyt-c include methionine sulfoxidation and tyrosine nitr...

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Detalles Bibliográficos
Autores principales: Capdevila, Daiana Andrea, Murgida, Daniel Horacio
Publicado: 2015
Materias:
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v54_n51_p7491_Capdevila
http://hdl.handle.net/20.500.12110/paper_00062960_v54_n51_p7491_Capdevila
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id paper:paper_00062960_v54_n51_p7491_Capdevila
record_format dspace
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Amino acids
Binding energy
Bins
Enzyme activity
Liposomes
Nitration
Oxidation
Phospholipids
Active site structure
Enzymatic activities
Lipid peroxidation
Peroxidase activities
Post-translational modifications
Proapoptotic signals
Tyrosine nitration
Wild-type proteins
Proteins
cardiolipin
cytochrome c
heme
liposome
methionine
peroxidase
protein variant
tyrosine
cardiolipin
cytochrome c
Article
conformational transition
controlled study
enzyme active site
enzyme activity
enzyme structure
excitation
lipid peroxidation
nitration
oxidative stress
priority journal
protein processing
protein protein interaction
Raman spectrometry
sulfoxidation
ultracentrifugation
ultraviolet spectroscopy
animal
chemistry
enzyme active site
horse
protein conformation
ultraviolet spectrophotometry
Animals
Cardiolipins
Catalytic Domain
Cytochromes c
Horses
Protein Conformation
Spectrophotometry, Ultraviolet
Spectrum Analysis, Raman
spellingShingle Amino acids
Binding energy
Bins
Enzyme activity
Liposomes
Nitration
Oxidation
Phospholipids
Active site structure
Enzymatic activities
Lipid peroxidation
Peroxidase activities
Post-translational modifications
Proapoptotic signals
Tyrosine nitration
Wild-type proteins
Proteins
cardiolipin
cytochrome c
heme
liposome
methionine
peroxidase
protein variant
tyrosine
cardiolipin
cytochrome c
Article
conformational transition
controlled study
enzyme active site
enzyme activity
enzyme structure
excitation
lipid peroxidation
nitration
oxidative stress
priority journal
protein processing
protein protein interaction
Raman spectrometry
sulfoxidation
ultracentrifugation
ultraviolet spectroscopy
animal
chemistry
enzyme active site
horse
protein conformation
ultraviolet spectrophotometry
Animals
Cardiolipins
Catalytic Domain
Cytochromes c
Horses
Protein Conformation
Spectrophotometry, Ultraviolet
Spectrum Analysis, Raman
Capdevila, Daiana Andrea
Murgida, Daniel Horacio
Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin
topic_facet Amino acids
Binding energy
Bins
Enzyme activity
Liposomes
Nitration
Oxidation
Phospholipids
Active site structure
Enzymatic activities
Lipid peroxidation
Peroxidase activities
Post-translational modifications
Proapoptotic signals
Tyrosine nitration
Wild-type proteins
Proteins
cardiolipin
cytochrome c
heme
liposome
methionine
peroxidase
protein variant
tyrosine
cardiolipin
cytochrome c
Article
conformational transition
controlled study
enzyme active site
enzyme activity
enzyme structure
excitation
lipid peroxidation
nitration
oxidative stress
priority journal
protein processing
protein protein interaction
Raman spectrometry
sulfoxidation
ultracentrifugation
ultraviolet spectroscopy
animal
chemistry
enzyme active site
horse
protein conformation
ultraviolet spectrophotometry
Animals
Cardiolipins
Catalytic Domain
Cytochromes c
Horses
Protein Conformation
Spectrophotometry, Ultraviolet
Spectrum Analysis, Raman
description We report a resonance Raman and UV-vis characterization of the active site structure of oxidatively modified forms of cytochrome c (Cyt-c) free in solution and in complexes with cardiolipin (CL). The studied post-translational modifications of Cyt-c include methionine sulfoxidation and tyrosine nitration, which lead to altered heme axial ligation and increased peroxidase activity with respect to those of the wild-type protein. In spite of the structural and activity differences between the protein variants free in solution, binding to CL liposomes induces in all cases the formation of a spectroscopically identical bis-His axial coordination conformer that more efficiently promotes lipid peroxidation. The spectroscopic results indicate that the bis-His form is in equilibrium with small amounts of high-spin species, thus suggesting a labile distal His ligand as the basis for the CL-induced increase in enzymatic activity observed for all protein variants. For Cyt-c nitrated at Tyr74 and sulfoxidized at Met80, the measured apparent binding affinities for CL are ∼4 times larger than for wild-type Cyt-c. On the basis of these results, we propose that these post-translational modifications may amplify the pro-apoptotic signal of Cyt-c under oxidative stress conditions at CL concentrations lower than for the unmodified protein. © 2015 American Chemical Society.
author Capdevila, Daiana Andrea
Murgida, Daniel Horacio
author_facet Capdevila, Daiana Andrea
Murgida, Daniel Horacio
author_sort Capdevila, Daiana Andrea
title Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin
title_short Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin
title_full Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin
title_fullStr Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin
title_full_unstemmed Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin
title_sort active site structure and peroxidase activity of oxidatively modified cytochrome c species in complexes with cardiolipin
publishDate 2015
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v54_n51_p7491_Capdevila
http://hdl.handle.net/20.500.12110/paper_00062960_v54_n51_p7491_Capdevila
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AT murgidadanielhoracio activesitestructureandperoxidaseactivityofoxidativelymodifiedcytochromecspeciesincomplexeswithcardiolipin
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