Enhanced Peroxidase Activity of Cytochrome c by Phosphate Bilayer Membrane

Fujita, Akio; Senzu, Hiroyuki; Kunitake, Toyoki; Hamachi, Itaru

doi:10.1246/cl.1994.1219

Cited by 36 publications

(27 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Additionally, in native cyt c the heme is deeply "buried" in the protein crevice, hence hindered access lowers peroxidase activity. 33,50,51 The two impacts of IL on cyt c, molecular expansion and ligand disturbance, should both enhance peroxidase activity. Table 1 shows the maximum slopes ∆A/∆t characterizing the steady state phase.…”

Section: Resultsmentioning

confidence: 99%

Dissolution and Dissolved State of Cytochrome c in a Neat, Hydrophilic Ionic Liquid

2010

View full text Add to dashboard Cite

The dissolution and dissolved molecular state of cytochrome c were investigated in the room temperature ionic liquid ethylmethylimidazolium ethylsulfate, [EMIM][EtSO4], by viscometry, optical and vibrational spectroscopies, and peroxidase activity. In dilute mixtures, viscometry demonstrated true molecular dissolution of cytochrome c in the ionic liquid and uncovered a molecular size larger than that in aqueous buffer, suggesting altered solvation or slight denaturation. The protein's heme unit absorbs light outside the spectral range masked by [EMIM], enabling conformational assessments by UV-visible and circular dichroism spectroscopies. Adding trends from fluorescence and Fourier transform infrared spectroscopy, unchanged secondary but perturbed tertiary structures were determined, consistent with the appreciable peroxidase activity measured. Different than in aqueous buffers, denaturation is not accompanied by aggregation. Results are relevant to the proposed application of ionic liquids as media for room temperature preservation of biomacromolecules.

show abstract

Section: Resultsmentioning

confidence: 99%

Dissolution and Dissolved State of Cytochrome c in a Neat, Hydrophilic Ionic Liquid

2010

View full text Add to dashboard Cite

show abstract

“…For instance, the binding of cytochrome c to a phosphate bilayer membrane and immobilizing it in reversed micelles is shown to enhance the peroxidase activity [62][63][64][65][66]. When the heme environment at the active site (namely the sixth coordination position of the heme) is altered by complexation with these modifiers, the substrate for peroxidation can access the active site of cytochrome c much easier than compared to its native state.…”

Section: (Iii) Catalytic Oxidation By the Cytochrome C Extracted In Omentioning

confidence: 99%

Recognition of Lysine Residues on Protein Surfaces Using Calixarenes and its Application

Oshima¹,

Baba²,

Shimojo³

et al. 2007

CDDT

View full text Add to dashboard Cite

A macrocyclic calix[6]arene carboxylic acid derivative is found to extract lysine-rich protein cytochrome c from aqueous media into organic media through the complexation between the calixarene molecules and lysine residues on the surface of the protein. This article summarizes both the mechanism of protein extraction by the calixarene as well as the potential applications of the extraction process. The extraction process can be used for the purification of proteins through selective extraction and back-extraction under optimized conditions. On the other hand, the extracted protein exhibits enzymatic activity in organic media. The formation of a supramolecular complex by recognizing the residues on a protein surface can be construed as a novel recognition and/or modification method for biomacromolecules.

show abstract

“…35 Although no catalytic activity of cyt c has been described in living systems, it was found to possess some peroxidase activity in vitro, especially when bound to lipid membrane. 36,37 The structure of the lipid is important to its peroxidase activity. 37 The possible reaction mechanism involves the generation of a high-valent oxioiron(IV) porphyrin radical cation from cyt c by the action of one molecule of hydrogen peroxide (H2O2).…”

Section: ·1 Cytochrome Cmentioning

confidence: 99%

“…36,37 The structure of the lipid is important to its peroxidase activity. 37 The possible reaction mechanism involves the generation of a high-valent oxioiron(IV) porphyrin radical cation from cyt c by the action of one molecule of hydrogen peroxide (H2O2). Other enzymatic activities, such as N-demethylase activity and cyt P450-like activity, have also been demonstrated upon incorporation in certain lipid membranes.…”

Section: ·1 Cytochrome Cmentioning

confidence: 99%

Third-Generation Biosensors Based on the Direct Electron Transfer of Proteins

Zhang

2004

ANAL. SCI.

173

View full text Add to dashboard Cite

Recent progress in third-generation electrochemical biosensors based on the direct electron transfer of proteins is reviewed. The development of three generations of electrochemical biosensors is also simply addressed. Special attention is paid to protein-film voltammetry, which is a powerful way to obtain the direct electron transfer of proteins. Research activities on various kinds of biosensors are discussed according to the proteins (enzymes) used in the specific work.

show abstract

Enhanced Peroxidase Activity of Cytochrome c by Phosphate Bilayer Membrane

Abstract: Peroxidase activity of cytochrome c (cyt-c) as measured by oxidation of o-methoxyphenol with H2O2, was enhanced due to binding of cyt-c to a phosphate bilayer membrane. The rate enhancement and the membrane binding were not observed with ammonium and zwitterionic bilayer membranes.

Cited by 36 publications

References 8 publications

Dissolution and Dissolved State of Cytochrome c in a Neat, Hydrophilic Ionic Liquid

Dissolution and Dissolved State of Cytochrome c in a Neat, Hydrophilic Ionic Liquid

Recognition of Lysine Residues on Protein Surfaces Using Calixarenes and its Application

Third-Generation Biosensors Based on the Direct Electron Transfer of Proteins

Contact Info

Product

Resources

About