Alternative Conformations of Cytochrome c: Structure, Function, and Detection

Cytochrome c (cyt c) is a cationic hemoprotein of ∼100 amino acid residues that exhibits exceptional functional versatility. While its primary function is electron transfer in the respiratory chain, cyt c is also recognized as a key component of the intrinsic apoptotic pathway, the mitochondrial oxi...

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Detalles Bibliográficos
Autores principales: Hannibal, L., Tomasina, F., Capdevila, D.A., Demicheli, V., Tórtora, V., Alvarez-Paggi, D., Jemmerson, R., Murgida, D.H., Radi, R.
Formato: JOUR
Materias:
Machinery
Phospholipids
Amino acid residues
Cellular compartments
Cellular homeostasis
Conformational change
Conformational state
Peroxidase activities
Post-translational modifications
Structural flexibilities
Amino acids
cardiolipin
cytochrome c
methionine
peroxidase
tyrosine
fungal protein
phospholipid
vegetable protein
antigenicity
apoptosis
cell respiration
circular dichroism
complex formation
conformational transition
crystal structure
electron transport
enzyme activity
genetic conservation
hydrogen bond
immunochemistry
in vitro study
membrane potential
nitration
oxidation reduction potential
phosphorylation
physical chemistry
priority journal
protein analysis
protein conformation
protein folding
protein function
protein phosphorylation
protein processing
protein secondary structure
protein stability
protein structure
respiratory chain
Review
static electricity
sulfoxidation
animal
chemistry
electricity
human
intracellular space
metabolism
protein transport
Animals
Cardiolipins
Cytochromes c
Electricity
Fungal Proteins
Humans
Intracellular Space
Plant Proteins
Protein Conformation
Protein Folding
Protein Processing, Post-Translational
Protein Transport
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00062960_v55_n3_p407_Hannibal
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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