Temperature, pH, and solvent isotope dependent properties of the active sites of resting-state and cyanide-ligated recombinant cytochrome c peroxidase (H52L) revealed by proton hyperfine resonance spectra

Biochemistry

Volumn 42, Issue 36, 2003, Pages 10772-10782

  Satterlee, James D ^a   Savenkova, Marina I ^a   Foshay, Miriam ^b   Erman, James E ^b  

^a WASHINGTON STATE UNIVERSITY   (United States)

^b NORTHERN ILLINOIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; COMPOSITION; ISOTOPES; NUCLEAR MAGNETIC RESONANCE; PH EFFECTS; SOLVENTS;

SOLVENT ISOTOPE COMPOSITION;

ENZYMES;

CYANIDE; CYTOCHROME C PEROXIDASE; HYDROGEN PEROXIDE; ISOTOPE; SOLVENT;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; LIGAND BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATIVE STRESS; PH; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; STRUCTURE ANALYSIS; TEMPERATURE; TITRIMETRY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; BINDING SITES; CYANIDES; CYTOCHROME-C PEROXIDASE; HEME; HISTIDINE; HYDROGEN-ION CONCENTRATION; LEUCINE; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTONS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SOLVENTS; TEMPERATURE;

EID: 0041469889     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034633c     Document Type: Article

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