Premium
Electrochemical Investigation of Cytochrome c Immobilized onto Self‐Assembled Monolayer of Captopril
Author(s) -
Alizadeh Vali,
Mehrgardi Masoud A.,
Fazlollah Mousavi Mir
Publication year - 2013
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.201300036
Subject(s) - cyclic voltammetry , monolayer , chemistry , electrochemistry , self assembled monolayer , dielectric spectroscopy , scanning electrochemical microscopy , electron transfer , electrode , analytical chemistry (journal) , redox , cytochrome c , scanning tunneling microscope , inorganic chemistry , photochemistry , nanotechnology , materials science , organic chemistry , biochemistry , mitochondrion
Abstract The electrochemical behavior of cytochrome c (cyt‐c) that was electrostatically immobilized onto a self‐assembled monolayer (SAM) of captopril (capt) on a gold electrode has been investigated. Cyclic voltammetry, scanning electrochemical microscopy (SECM) and electrochemical impedance spectroscopy were employed to evaluate the blocking property of the capt SAM. SECM was used to measure the bimolecular electron transfer (ET) kinetics ( k BI ) between a solution‐based redox probe and the immobilized protein. In addition, the tunneling ET between the immobilized protein and the underlying gold electrode was calculated. A k BI value of (5.0±0.6)×10 8 mol −1 cm 3 s −1 for the bimolecular ET and a standard tunneling rate constant ( k 0 ) of 46.4±0.2 s −1 for the tunneling ET have been obtained.