The crucial importance of chemistry in the structure-function link: Manipulating hydrogen bonding in iron-containing superoxide dismutase

Biochemistry

Volumn 45, Issue 4, 2006, Pages 1151-1161

  Yikilmaz, Emine ^a,b,d   Rodgers, David W ^c   Miller, Anne Frances ^a,b,c  

^a UNIVERSITY OF KENTUCKY   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

^c UNIVERSITY OF KENTUCKY MEDICAL CENTER   (United States)

^d BAYER AG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS; IRON; MUTAGENESIS; PROTONS; REDOX REACTIONS; SOLVENTS;

MUTATIONS; PROTONATION STATES; REDOX TITRATIONS; SUPEROXIDE DISMUTASE (SOD);

ENZYMES;

GLUTAMINE; GLYCINE; HISTIDINE; IRON; IRON SUPEROXIDE DISMUTASE; SOLVENT;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; HYDROGEN BOND; OXIDATION; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTON TRANSPORT; STRUCTURE ANALYSIS; TITRIMETRY; X RAY DIFFRACTION;

AMINO ACID SUBSTITUTION; BINDING SITES; CRYSTALLIZATION; ESCHERICHIA COLI; GLUTAMIC ACID; GLYCINE; HISTIDINE; HYDROGEN BONDING; IRON; KINETICS; MODELS, MOLECULAR; MUTATION; OXIDATION-REDUCTION; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; SUPEROXIDE DISMUTASE;

EID: 31544448000     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051495d     Document Type: Article

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