Enhancing stability and oxidation activity of cytochrome c by immobilization in the nanochannels of mesoporous aluminosilicates

Chia Hung Lee; Jun Lang; Chun Wan Yen; Pei Chun Shih; Tien Sung Lin; Chung Yuan Mou

doi:10.1021/jp050535k

Enhancing stability and oxidation activity of cytochrome c by immobilization in the nanochannels of mesoporous aluminosilicates

Chia Hung Lee, Jun Lang, Chun Wan Yen, Pei Chun Shih, Tien Sung Lin, Chung Yuan Mou

Research output: Contribution to journal › Article › peer-review

101 Citations (Scopus)

Abstract

The hydrothermal stability and oxidation activity of cytochrome c (cty c) by immobilization in the nanochannels of mesoporous aluminosilicates were discussed. The cytochrome c immobilized in MAS-9 undergo facile unfolding during hydrothermal stability. The stability and high catalytic activity of cyt c immobilized in mesoporous silicas were attributed to the electrostatic attraction between the pore surface and cyt c and the confinement provided by nanochannels. It was found that by increasing the concentration of the spin trapping agent, cyt c catalyzes a homolytic cleavage of the O-O bond of hydroperoxide and generates a protein cation radicals.

Original language	English
Pages (from-to)	12277-12286
Number of pages	10
Journal	Journal of Physical Chemistry B
Volume	109
Issue number	25
DOIs	https://doi.org/10.1021/jp050535k
Publication status	Published - Jun 30 2005
Externally published	Yes

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Surfaces, Coatings and Films
Materials Chemistry

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title = "Enhancing stability and oxidation activity of cytochrome c by immobilization in the nanochannels of mesoporous aluminosilicates",

abstract = "The hydrothermal stability and oxidation activity of cytochrome c (cty c) by immobilization in the nanochannels of mesoporous aluminosilicates were discussed. The cytochrome c immobilized in MAS-9 undergo facile unfolding during hydrothermal stability. The stability and high catalytic activity of cyt c immobilized in mesoporous silicas were attributed to the electrostatic attraction between the pore surface and cyt c and the confinement provided by nanochannels. It was found that by increasing the concentration of the spin trapping agent, cyt c catalyzes a homolytic cleavage of the O-O bond of hydroperoxide and generates a protein cation radicals.",

author = "Lee, \{Chia Hung\} and Jun Lang and Yen, \{Chun Wan\} and Shih, \{Pei Chun\} and Lin, \{Tien Sung\} and Mou, \{Chung Yuan\}",

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T1 - Enhancing stability and oxidation activity of cytochrome c by immobilization in the nanochannels of mesoporous aluminosilicates

AU - Lee, Chia Hung

AU - Lang, Jun

AU - Yen, Chun Wan

AU - Shih, Pei Chun

AU - Lin, Tien Sung

AU - Mou, Chung Yuan

PY - 2005/6/30

Y1 - 2005/6/30

N2 - The hydrothermal stability and oxidation activity of cytochrome c (cty c) by immobilization in the nanochannels of mesoporous aluminosilicates were discussed. The cytochrome c immobilized in MAS-9 undergo facile unfolding during hydrothermal stability. The stability and high catalytic activity of cyt c immobilized in mesoporous silicas were attributed to the electrostatic attraction between the pore surface and cyt c and the confinement provided by nanochannels. It was found that by increasing the concentration of the spin trapping agent, cyt c catalyzes a homolytic cleavage of the O-O bond of hydroperoxide and generates a protein cation radicals.

AB - The hydrothermal stability and oxidation activity of cytochrome c (cty c) by immobilization in the nanochannels of mesoporous aluminosilicates were discussed. The cytochrome c immobilized in MAS-9 undergo facile unfolding during hydrothermal stability. The stability and high catalytic activity of cyt c immobilized in mesoporous silicas were attributed to the electrostatic attraction between the pore surface and cyt c and the confinement provided by nanochannels. It was found that by increasing the concentration of the spin trapping agent, cyt c catalyzes a homolytic cleavage of the O-O bond of hydroperoxide and generates a protein cation radicals.

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AN - SCOPUS:22744457649

SN - 1520-6106

VL - 109

SP - 12277

EP - 12286

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 25

ER -

Enhancing stability and oxidation activity of cytochrome c by immobilization in the nanochannels of mesoporous aluminosilicates

Abstract

ASJC Scopus subject areas

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