A bis-histidine-ligated unfolded cytochrome c immobilized on anionic SAM shows pseudo-peroxidase activity

Ranieri, Antonio; Battistuzzi, Gianantonio; Borsari, Marco; Bortolotti, Carlo Augusto; Rocco, Giulia Di; Monari, Stefano; Sola, Marcó

doi:10.1016/j.elecom.2011.10.021

Cited by 32 publications

(59 citation statements)

References 27 publications

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“…However, there are several reports on different heme‐protein‐modified electrodes that describe the peroxide reduction at the potential in which the heme is in the reduced state. In analogy to unfolded cytochrome c,19 the reaction with peroxide could lead through Fe II to Fe IV O for HTHP as well 20. This species has a remarkably more positive formal potential than the ferric heme and it is immediately reduced at this potential along with the reduction of ferric HTHP.…”

Section: Resultsmentioning

confidence: 99%

Surface‐Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine‐Coordinated Heme Protein

Peng

Utesch

Yarman

et al. 2015

Chemistry A European J

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Molecular modeling, electrochemical methods, and quartz crystal microbalance were used to characterize immobilized hexameric tyrosine-coordinated heme protein (HTHP) on bare carbon or on gold electrodes modified with positively and negatively charged self-assembled monolayers (SAMs), respectively. HTHP binds to the positively charged surface but no direct electron transfer (DET) is found due to the long distance of the active sites from the electrode surfaces. At carboxyl-terminated surfaces, the neutrally charged bottom of HTHP can bind to the SAM. For this "disc" orientation all six hemes are close to the electrode and their direct electron transfer should be efficient. HTHP on all negatively charged SAMs showed a quasi-reversible redox behavior with rate constant ks values between 0.93 and 2.86 s(-1) and apparent formal potentials ${E{{0{^{\prime }}\hfill \atop {\rm app}\hfill}}}$ between -131.1 and -249.1 mV. On the MUA/MU-modified electrode, the maximum surface concentration corresponds to a complete monolayer of the hexameric HTHP in the disc orientation. HTHP electrostatically immobilized on negatively charged SAMs shows electrocatalysis of peroxide reduction and enzymatic oxidation of NADH.

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Section: Resultsmentioning

confidence: 99%

Surface‐Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine‐Coordinated Heme Protein

Peng

Utesch

Yarman

et al. 2015

Chemistry A European J

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“…According to the reported, the exposure of heme cofactor to solvent and the nature of the axial ligand seems to be the principal determinant for the magnitude of the formal potential 40,47,48. According to the reported, the exposure of heme cofactor to solvent and the nature of the axial ligand seems to be the principal determinant for the magnitude of the formal potential 40,47,48.…”

mentioning

confidence: 94%

Label-Free Surface-Enhanced Infrared Spectroelectrochemistry Studies the Interaction of Cytochrome c with Cardiolipin-Containing Membranes

Liu

Zeng

et al. 2015

J. Phys. Chem. C

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Interactions of cytochrome c (cyt c) with cardiolipin (CL)-containing membranes have been revealed to play an important role in inducing early apoptosis. In this paper, we studied the interaction of cyt c with solid-supported CL-containing lipid bilayers by a lable-free spectroelectrochemistry method. The biomimetic membrane was fabricated by fusing cardiolipin-phosphatidylcholine (CL_PC, 1:4) vesicles onto the hydrophobic surface of a preadsorbed 1-dodecanethiol (DT) on a gold electrode (CL_PC/DT/Au). The adsorption of cyt c onto the CL_PC/DT/Au was in-situ studied by cyclic voltammetry (CV) and surface-enhanced Infrared adsorption spectroscopy (SEIRAS). The electrochemistry of Cyt c/CL_PC/DT/Au exhibits the formal potential (E f ) at 0.21 V (vs. Ag/AgCl), a positive shift of 190 mV as compared to that of native cyt c adsorbed at the mercaptoundecanoic acid-modified gold Page 1 of 34 ACS Paragon Plus Environment The Journal of Physical Chemistry 2 electrode (Cyt c/MUA/Au). The potential-induced SEIRA difference spectroscopy discloses that cyt c was loosely adsorbed onto CL_PC/DT/Au in a different orientation, and underwent a new β-sheet formation relative to native cyt c adsorbed onto MUA/Au. It could be the enhanced hydration change of CL-bound cyt c upon oxidization and reduction and the different adsorption orientation that determine the positive shift in its formal potential.

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“…On the other hand, there is a large number of reports describing the peroxide reduction at the potential where the heme is in the reduced state. In analogy to unfolded cytochrome c [ 28 ] also for microperoxidase the reaction with peroxide could lead via Fe(II) to Fe(IV) = O [ 29 ]. This species has a remarkably more positive formal potential than the ferric heme and it is immediately reduced at this potential along with the reduction of ferric microperoxidase.…”

Section: Resultsmentioning

confidence: 99%

Peroxide-Dependent Analyte Conversion by the Heme Prosthetic Group, the Heme Peptide “Microperoxidase-11” and Cytochrome c on Chitosan Capped Gold Nanoparticles Modified Electrodes

et al. 2012

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In view of the role ascribed to the peroxidatic activity of degradation products of cytochrome c (cyt c) in the processes of apoptosis, we investigate the catalytic potential of heme and of the cyt c derived heme peptide MP-11 to catalyse the cathodic reduction of hydrogen peroxide and to oxidize aromatic compounds. In order to check whether cyt c has an enzymatic activity in the native state where the protein matrix should suppress the inherent peroxidatic activity of its heme prosthetic group, we applied a biocompatible immobilization matrix and very low concentrations of the co-substrate H2O2. The biocatalysts were entrapped on the surface of a glassy carbon electrode in a biocompatible chitosan layer which contained gold nanoparticles. The electrochemical signal for the peroxide reduction is generated by the redox conversion of the heme group, whilst a reaction product of the substrate oxidation is cathodically reduced in the substrate indication. The catalytic efficiency of microperoxidase-11 is sufficient for sensors indicating HRP substrates, e.g., p-aminophenol, paracetamol and catechol, but also the hydroxylation of aniline and dehalogenation of 4-fluoroaniline. The lower limit of detection for p-aminophenol is comparable to previously published papers with different enzyme systems. The peroxidatic activity of cyt c immobilized in the chitosan layer for catechol was found to be below 1 per mill and for p-aminophenol about 3% as compared with that of heme or MP-11.

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A bis-histidine-ligated unfolded cytochrome c immobilized on anionic SAM shows pseudo-peroxidase activity

Cited by 32 publications

References 27 publications

Surface‐Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine‐Coordinated Heme Protein

Surface‐Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine‐Coordinated Heme Protein

Label-Free Surface-Enhanced Infrared Spectroelectrochemistry Studies the Interaction of Cytochrome c with Cardiolipin-Containing Membranes

Peroxide-Dependent Analyte Conversion by the Heme Prosthetic Group, the Heme Peptide “Microperoxidase-11” and Cytochrome c on Chitosan Capped Gold Nanoparticles Modified Electrodes

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