The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status

Journal of Biological Chemistry

Volumn 279, Issue 46, 2004, Pages 47998-48003

  Arnesano, Fabio ^a   Banci, Lucia ^a   Bertini, Ivano ^a   Martinelli, Manuele ^a   Furukawa, Yoshiaki ^b   O'Halloran, Thomas V ^b  

^a UNIVERSITY OF FLORENCE   (Italy)

^b NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELLS; CHEMICAL BONDS; CONCENTRATION (PROCESS); COPPER; MONOMERS; MUTAGENESIS; ZINC;

CYTOSOL; DISULFIDE BONDS; QUATERNARY STRUCTURES; SUPEROXIDE DISMUTASES;

ENZYMES;

COPPER ZINC SUPEROXIDE DISMUTASE; DIMER; DISULFIDE; METAL; MONOMER; ZINC;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; BIOPHYSICS; EQUILIBRIUM CONSTANT; MITOCHONDRION; MUTANT; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

CIRCULAR DICHROISM; COPPER; DIMERIZATION; DISULFIDES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SUPEROXIDE DISMUTASE; ZINC;

EUKARYOTA;

EID: 9144261759     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M406021200     Document Type: Article

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