Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: Evidence for a single, catalytically active, cytochrome c binding domain

Biochemistry

Volumn 47, Issue 9, 2008, Pages 2766-2775

  Pearl, Naw May ^a   Jacobson, Timothy ^a   Meyen, Cassandra ^a   Clementz, Anthony G ^a   Ok, Esther Y ^a   Choi, Eric ^a   Wilson, Kyle ^a   Vitello, Lidia B ^a   Erman, James E ^a  

^a NORTHERN ILLINOIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION SPECTROSCOPY; BINDING SITES; CATALYST ACTIVITY; CRYSTALLOGRAPHY; MUTAGENS; YEAST;

CHARGE-REVERSAL MUTATIONS; GLUTAMATE RESIDUES; ISO-1 FERROCYTOCHROME C (C102T);

ENZYMES;

ASPARTIC ACID; CYTOCHROME C; CYTOCHROME C PEROXIDASE; GLUTAMIC ACID; HEME; HYDROGEN PEROXIDE; LYSINE; RECOMBINANT PROTEIN;

ABSORPTION SPECTROSCOPY; ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL REACTION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME LOCALIZATION; MICHAELIS CONSTANT; MUTANT; MUTATION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; STEADY STATE; SURFACE CHARGE; VELOCITY; WILD TYPE; YEAST;

BINDING SITES; CATALYSIS; CYTOCHROME-C PEROXIDASE; CYTOCHROMES C; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURE-ACTIVITY RELATIONSHIP; YEASTS;

EID: 40149111566     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702271r     Document Type: Article

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