Probing of enzyme reactions by the biocatalyst-induced association or dissociation of redox labels linked to monolayer-functionalized electrodes.
The activities of the enzymes tyrosinase and thrombin are probed by the association of the ferrocene boronic acid label to the enzyme-generated catechol ligand, and by the cleavage of the ligand-redox complex tethered to a peptide, respectively.
Li
Di
D
Institute of Chemistry, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel.
Gill
Ron
R
Freeman
Ronit
R
Willner
Itamar
I
D015374:Biosensing Techniques / Q000295:instrumentation / Q000379:methods*; D002396:Catechols / Q000737:chemistry*; D004295:Dihydroxyphenylalanine / Q000737:chemistry; D004563:Electrochemistry; D004566:Electrodes; D005296:Ferrous Compounds / Q000737:chemistry*; D015394:Molecular Structure; D014442:Monophenol Monooxygenase / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry; D010084:Oxidation-Reduction; D013917:Thrombin / Q000737:chemistry*; D014439:Tyramine / Q000737:chemistry
D002396:Catechols; D005296:Ferrous Compounds; D009842:Oligopeptides; C420283:ferrocenyl boronate; D004295:Dihydroxyphenylalanine; D014442:Monophenol Monooxygenase; D013917:Thrombin; D014439:Tyramine