Redox behavior of human serum albumin-heme hybrid on graphite electrode modified with didodecyldimethylammonium bromide

Yuping Wu; Teruyuki Komatsu; Eishun Tsuchida

doi:10.1246/cl.2000.1194

Redox behavior of human serum albumin-heme hybrid on graphite electrode modified with didodecyldimethylammonium bromide

Yuping Wu, Teruyuki Komatsu, Eishun Tsuchida

Waseda University

科研成果: 期刊稿件 › 文章 › 同行评审

2 引用（Scopus）

摘要

The redox behavior of a synthetic hemoprotein, the recombinant human serum albumin (rHSA), incorporating a tetraphenylporphinatoiron derivative (FeP) [rHSA-FeP] was first evaluated using a graphite electrode modified with didodecyldimethylammonium bromide as a promoter. Compared to that of the naked FeP, the redox potential of the Fe(III)/Fe(II) couple in rHSA-FeP shifts in the positive direction, indicating that the central ferrous ion of FeP becomes more difficult to be oxidized by incorporation into the albumin structure.

源语言	英语
页（从-至）	1194-1195
页数	2
期刊	Chemistry Letters
期	10
DOI	https://doi.org/10.1246/cl.2000.1194
出版状态	已出版 - 2000
已对外发布	是

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title = "Redox behavior of human serum albumin-heme hybrid on graphite electrode modified with didodecyldimethylammonium bromide",

abstract = "The redox behavior of a synthetic hemoprotein, the recombinant human serum albumin (rHSA), incorporating a tetraphenylporphinatoiron derivative (FeP) [rHSA-FeP] was first evaluated using a graphite electrode modified with didodecyldimethylammonium bromide as a promoter. Compared to that of the naked FeP, the redox potential of the Fe(III)/Fe(II) couple in rHSA-FeP shifts in the positive direction, indicating that the central ferrous ion of FeP becomes more difficult to be oxidized by incorporation into the albumin structure.",

author = "Yuping Wu and Teruyuki Komatsu and Eishun Tsuchida",

year = "2000",

doi = "10.1246/cl.2000.1194",

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journal = "Chemistry Letters",

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AU - Wu, Yuping

AU - Komatsu, Teruyuki

AU - Tsuchida, Eishun

PY - 2000

Y1 - 2000

N2 - The redox behavior of a synthetic hemoprotein, the recombinant human serum albumin (rHSA), incorporating a tetraphenylporphinatoiron derivative (FeP) [rHSA-FeP] was first evaluated using a graphite electrode modified with didodecyldimethylammonium bromide as a promoter. Compared to that of the naked FeP, the redox potential of the Fe(III)/Fe(II) couple in rHSA-FeP shifts in the positive direction, indicating that the central ferrous ion of FeP becomes more difficult to be oxidized by incorporation into the albumin structure.

AB - The redox behavior of a synthetic hemoprotein, the recombinant human serum albumin (rHSA), incorporating a tetraphenylporphinatoiron derivative (FeP) [rHSA-FeP] was first evaluated using a graphite electrode modified with didodecyldimethylammonium bromide as a promoter. Compared to that of the naked FeP, the redox potential of the Fe(III)/Fe(II) couple in rHSA-FeP shifts in the positive direction, indicating that the central ferrous ion of FeP becomes more difficult to be oxidized by incorporation into the albumin structure.

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DO - 10.1246/cl.2000.1194

M3 - 文章

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EP - 1195

JO - Chemistry Letters

JF - Chemistry Letters

IS - 10

ER -

Redox behavior of human serum albumin-heme hybrid on graphite electrode modified with didodecyldimethylammonium bromide

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