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, D.A., Oviedo Rouco, S., Tomasina, F., Tortora, V., Demicheli, V., Radi, R., Murgida, D.H.
Formato: JOUR
Materias:
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
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
horse
protein conformation
ultraviolet spectrophotometry
Animals
Cardiolipins
Catalytic Domain
Cytochromes c
Horses
Protein Conformation
Spectrophotometry, Ultraviolet
Spectrum Analysis, Raman
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00062960_v54_n51_p7491_Capdevila
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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