Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein

Journal of the American Chemical Society

Volumn 129, Issue 15, 2007, Pages 4575-4583

  Potter, Soshanna Zittin ^a   Zhu, Haining ^b   Shaw, Bryan Francis ^a   Rodriguez, Jorge A ^a   Doucette, Peter A ^a   Se, Hui Sohn ^a   Durazo, Armando ^a   Faull, Kym F ^a   Gralla, Edith Butler ^a   Nersissian, Aram M ^c   Valentine, Joan Selverstone ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

^c OCCIDENTAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; DIFFERENTIAL SCANNING CALORIMETRY; HYDROGEN; ISOTHERMS; MONOMERS; STABILITY; TITRATION; ZINC;

HOMODIMERS; ISOTHERMAL TITRATION CALORIMETRY; SUPEROXIDES; THERMOSTABILITY;

PROTEINS;

APOPROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; HOMODIMER;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; HUMAN; ISOTHERMAL TITRATION CALORIMETRY; METAL BINDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; STOICHIOMETRY; THERMODYNAMICS; THERMOSTABILITY; ULTRACENTRIFUGATION;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; APOPROTEINS; CATIONS; CATTLE; CHEMISTRY, PHYSICAL; DIMERIZATION; HUMANS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; SUPEROXIDE DISMUTASE; THERMODYNAMICS; ZINC;

EID: 34247505040     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja066690+     Document Type: Article

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