Enzymatic activity and catalytic hydrogen evolution in reduced and oxidized urease at mercury surfaces

Analytica Chimica Acta

Volumn 789, Issue , 2013, Pages 41-46

  Černocká, Hana ^a   Ostatná, Veronika ^a   Paleček, Emil ^a,b  

^a INSTITUTE OF BIOPHYSICS   (Czech Republic)

^b MASARYK MEMORIAL CANCER INSTITUTE   (Czech Republic)

Author keywords

Constant current chronopotentiometric stripping; Mercury containing electrodes; Protein denaturation at negatively charged surfaces; Protein structure at surfaces; Thiol modified electrodes; Urease enzymatic activity

Indexed keywords

CATALYTIC HYDROGEN EVOLUTION; CONSTANT-CURRENT; DISULFIDE BONDS; ENZYMATIC ACTIVITIES; NEGATIVE POTENTIAL; NEGATIVELY CHARGED SURFACES; PROTEIN STRUCTURES; PROTEIN UNFOLDING;

AMINO ACIDS; COVALENT BONDS; ELECTRIC FIELD EFFECTS; ELECTRODES; ENZYME ACTIVITY; MERCURY (METAL); REDUCTION;

PROTEINS;

AMALGAM; MERCURY; UREASE;

ADSORPTION; ARTICLE; CATALYSIS; CURRENT CHRONOPOTENTIOMETRIC STRIPPING; DISULFIDE BOND; ELECTRIC FIELD; ELECTRODE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME METABOLISM; HYDROGEN EVOLUTION; POTENTIOMETRY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE;

CONSTANT-CURRENT CHRONOPOTENTIOMETRIC STRIPPING; MERCURY CONTAINING ELECTRODES; PROTEIN DENATURATION AT NEGATIVELY CHARGED SURFACES; PROTEIN STRUCTURE AT SURFACES; THIOL-MODIFIED ELECTRODES; UREASE ENZYMATIC ACTIVITY;

ADSORPTION; CATALYSIS; CYSTEINE; DISULFIDES; DITHIOTHREITOL; ELECTROCHEMICAL TECHNIQUES; ELECTRODES; MERCURY; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN FOLDING; SULFHYDRYL COMPOUNDS; SURFACE PROPERTIES; TEMPERATURE; UREASE;

EID: 84880317236     PISSN: 00032670     EISSN: 18734324     Source Type: Journal    
DOI: 10.1016/j.aca.2013.06.014     Document Type: Article

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