How active-site protonation state influences the reactivity and ligation of the heme in chlorite dismutase

Journal of the American Chemical Society

Volumn 132, Issue 16, 2010, Pages 5711-5724

  Streit, Bennett R ^a   Blanc, Béatrice ^a   Lukat Rodgers, Gudrun S ^b   Rodgers, Kenton R ^b   Dubois, Jennifer L ^a  

^a UNIVERSITY OF NOTRE DAME   (United States)

^b NORTH DAKOTA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACID BASE; ALKALINE CONDITIONS; ALKALINE HYDROXIDE; ANALOGOUS TRANSITIONS; BINDING REACTIONS; CARBONYL OXYGEN; CRYSTALLOGRAPHIC DATA; DIOXYGENS; DISMUTASE; DISTAL POCKET; ENVIRONMENT INFLUENCE; FERRIC HYDROXIDE; GAIN INSIGHT; HISTIDINE LIGANDS; LIGAND BINDING AFFINITY; MINIMAL INTERACTIONS; NEUTRAL IMIDAZOLE; O-H BOND; POSITIVE CHARGES; POSITIVELY CHARGED; PROTONATED; PROTONATION STATE; RESONANCE RAMAN SPECTROSCOPY; SIDE CHAINS; SPECTROSCOPIC PROPERTY; STEADY STATE PROFILES; STEADY-STATE KINETICS; STRETCHING FREQUENCY; TRANSITION MARKS;

ACIDS; AMINO ACIDS; BINDING ENERGY; HEMOGLOBIN; IRON COMPOUNDS; OXYGEN; PHOSPHATASES; PLANTS (BOTANY); PORPHYRINS; PROTONATION; SPIN DYNAMICS;

LIGANDS;

ARGININE; CARBONYL DERIVATIVE; CHLORITE DISMUTASE; FERRIC HYDROXIDE; FERRIC ION; HEME; HEME DERIVATIVE; HISTIDINE; HYDROGEN; IMIDAZOLE DERIVATIVE; OXYGEN; PEROXIDASE; UNCLASSIFIED DRUG; CARBON MONOXIDE; LIGAND; OXIDOREDUCTASE; PROTON;

ARTICLE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; HYDROGEN BOND; LIGATION; NONHUMAN; PH; PROTON TRANSPORT; RAMAN SPECTROMETRY; SPIN LABELING; STEADY STATE; ULTRAVIOLET RADIATION; VIBRATION; BIOCATALYSIS; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; HYDROPHOBICITY; KINETICS; METABOLISM; PROTEIN BINDING; RHODOCYCLACEAE; ULTRAVIOLET SPECTROPHOTOMETRY;

BIOCATALYSIS; CARBON MONOXIDE; CATALYTIC DOMAIN; ENZYME STABILITY; HEME; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; KINETICS; LIGANDS; OXIDOREDUCTASES; PROTEIN BINDING; PROTONS; RHODOCYCLACEAE; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN;

EID: 77952558152     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja9082182     Document Type: Article

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