A FRET-based biosensor for NO detection

被引：19

作者：

Strianese, Maria ^{[2
]}

De Martino, Franco ^{[2
]}

Pavone, Vincenzo ^{[3
]}

Lombardi, Angela ^{[3
]}

Canters, Gerard W. ^{[1
]}

Pellecchia, Claudio ^{[2
]}

机构：

[1] Leiden Univ, Leiden Inst Chem, NL-2333 CC Leiden, Netherlands

[2] Univ Salerno, Dipartimento Chim, I-84084 Fisciano, Sa, Italy

[3] Univ Naples Federico II, Dipartimento Chim, I-80126 Naples, Italy

来源：

JOURNAL OF INORGANIC BIOCHEMISTRY | 2010年 / 104卷 / 06期

关键词：

Heme proteins; Biosensors; Fluorescence; FRET; Sol-gel processes; CYTOCHROME-C PEROXIDASE; NITRIC-OXIDE CONCENTRATIONS; ENERGY-TRANSFER; CELLULAR APPLICATIONS; TUMOR PROGRESSION; BINDING; YEAST; LIPOPOLYSACCHARIDE; COORDINATION; GENERATION;

D O I：

10.1016/j.jinorgbio.2010.02.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In this paper we explore the use of fluorescently labeled cytochrome c peroxidase (CcP) from baker's yeast for monitoring nitric oxide (NO) down to the sub-micromolar level, by means of a FRET (Forster Resonance Energy Transfer) mechanism. The binding affinity constant (K-d) for the NO binding to CcP was determined to be 10 +/- 1.5 mu M. The rate of NO dissociation from the CcP (k(off)) and the second order rate constant for the NO association (k(on)) were found to be 0.22 +/- 0.08 min(-1) and 0.024 +/- 0.002 mu M-1 min(-1) respectively. The immobilization of fluorescently labeled CcP into a polymeric matrix for use in a solid state NO sensing device was also explored. The results provide proof-of-principle that labeled CcP can be successfully implemented in a fast, simple, quantitative and sensitive NO sensing device. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：619 / 624

页数：6

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