Human recombinant mutated forms of the mitochondrial COX assembly Sco2 protein differ from wild-type in physical state and copper binding capacity

Molecular Genetics and Metabolism

Volumn 81, Issue 3, 2004, Pages 225-236

  Foltopoulou, Parthena F ^a   Zachariadis, George A ^a   Politou, Anastasia S ^b   Tsiftsoglou, Asterios S ^a   Papadopoulou, Lefkothea C ^a  

^a ARISTOTLE UNIVERSITY OF THESSALONIKI   (Greece)

^b UNIVERSITY OF IOANNINA   (Greece)

Author keywords

Conformation; COX deficiency; Mitochondrial copper pathway; Mutations; RhSco2p

Indexed keywords

COPPER; DIMER; MITOCHONDRIAL ENZYME; MONOMER; MUTANT PROTEIN; PEPTIDE; PROSTAGLANDIN SYNTHASE; PROTEIN; PROTEIN SCO2; RECOMBINANT ENZYME; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BRAIN DISEASE; CARDIOMYOPATHY; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ASSAY; ENZYME DEFICIENCY; HUMAN; METABOLIC DISORDER; METAL BINDING; MITOCHONDRIAL RESPIRATION; MOLECULAR DYNAMICS; MUTATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN TRANSPORT; TEMPERATURE DEPENDENCE; WILD TYPE;

EID: 1242270485     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ymgme.2003.11.006     Document Type: Article

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