Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34

Biochemistry

Volumn 44, Issue 16, 2005, Pages 5969-5981

  Miller, Anne Frances ^a,b   Sorkin, David L ^a   Padmakumar, K ^b  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; HYDROGEN BONDS; IRON; NEGATIVE IONS; PH EFFECTS; PROTONS; REDOX REACTIONS; RELAXATION PROCESSES; SOLVENTS; SPECTROSCOPIC ANALYSIS;

ANION BINDING; IRON SUPEROXIDE; NUCLEAR MAGNETIC RELAXATION DISPERSION (NMRD); STERIC INTERFERENCE;

ENZYME INHIBITION;

ANION; IRON SUPEROXIDE DISMUTASE; PROTON; TYROSINE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROGEN BOND; MATHEMATICAL ANALYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OXIDATION; PH; PRIORITY JOURNAL; SPECTROSCOPY;

AMINO ACID SUBSTITUTION; ANIONS; CATALYTIC DOMAIN; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; IRON; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; SUPEROXIDE DISMUTASE; THERMODYNAMICS; TYROSINE;

ESCHERICHIA COLI;

EID: 17644424319     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0476331     Document Type: Article

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