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Direct electrochemistry of hemoglobin in PHEA and its catalysis to H2O2.
Biosens Bioelectron. 2007 Jan 15; 22(6):899-904.BB

Abstract

Hemoglobin (Hb) was immobilized on glassy carbon (GC) electrode by a kind of synthetic water-soluble polymer, poly-alpha,beta-[N-(2-hydroxyethyl)-L-aspartamide] (PHEA). A pair of well-defined and quasi-reversible cyclic voltammetric peaks was achieved, which reflected the direct electron-transfer of the Fe(III)/Fe(II) couple of Hb. The formal potential (E degrees'), the apparent coverage (Gamma(*)) and the electron-transfer rate constant (k(s)) were calculated by integrating cyclic voltammograms experimental data. Scanning electron microscopy (SEM) demonstrated the morphology of Hb-PHEA film very different from the Hb and PHEA films. Ultraviolet visible (UV-vis) spectroscopy showed Hb in PHEA film remained its secondary structure similar to the native state. In respect that the immobilized protein remained its biocatalytic activity to the reduction of hydrogen peroxide (H(2)O(2)), a kind of mediator-free biosensor for H(2)O(2) could be developed. The apparent Michaelis-Menten constant (K(m)(app)) was estimated to be 18.05 microM. The biosensor exhibited rapid electrochemical response and good stability. Furthermore, uric acid (UA), ascorbic acid (AA) and dopamine (DA) had little interferences with the amperometric signal of H(2)O(2), which provide the perspective of this H(2)O(2) sensor to be used in biological environments.

Authors+Show Affiliations

College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16621505

Citation

Lu, Qing, et al. "Direct Electrochemistry of Hemoglobin in PHEA and Its Catalysis to H2O2." Biosensors & Bioelectronics, vol. 22, no. 6, 2007, pp. 899-904.
Lu Q, Zhou T, Hu S. Direct electrochemistry of hemoglobin in PHEA and its catalysis to H2O2. Biosens Bioelectron. 2007;22(6):899-904.
Lu, Q., Zhou, T., & Hu, S. (2007). Direct electrochemistry of hemoglobin in PHEA and its catalysis to H2O2. Biosensors & Bioelectronics, 22(6), 899-904.
Lu Q, Zhou T, Hu S. Direct Electrochemistry of Hemoglobin in PHEA and Its Catalysis to H2O2. Biosens Bioelectron. 2007 Jan 15;22(6):899-904. PubMed PMID: 16621505.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Direct electrochemistry of hemoglobin in PHEA and its catalysis to H2O2. AU - Lu,Qing, AU - Zhou,Tao, AU - Hu,Shengshui, Y1 - 2006/04/18/ PY - 2006/01/09/received PY - 2006/03/04/revised PY - 2006/03/14/accepted PY - 2006/4/20/pubmed PY - 2007/3/7/medline PY - 2006/4/20/entrez SP - 899 EP - 904 JF - Biosensors & bioelectronics JO - Biosens Bioelectron VL - 22 IS - 6 N2 - Hemoglobin (Hb) was immobilized on glassy carbon (GC) electrode by a kind of synthetic water-soluble polymer, poly-alpha,beta-[N-(2-hydroxyethyl)-L-aspartamide] (PHEA). A pair of well-defined and quasi-reversible cyclic voltammetric peaks was achieved, which reflected the direct electron-transfer of the Fe(III)/Fe(II) couple of Hb. The formal potential (E degrees'), the apparent coverage (Gamma(*)) and the electron-transfer rate constant (k(s)) were calculated by integrating cyclic voltammograms experimental data. Scanning electron microscopy (SEM) demonstrated the morphology of Hb-PHEA film very different from the Hb and PHEA films. Ultraviolet visible (UV-vis) spectroscopy showed Hb in PHEA film remained its secondary structure similar to the native state. In respect that the immobilized protein remained its biocatalytic activity to the reduction of hydrogen peroxide (H(2)O(2)), a kind of mediator-free biosensor for H(2)O(2) could be developed. The apparent Michaelis-Menten constant (K(m)(app)) was estimated to be 18.05 microM. The biosensor exhibited rapid electrochemical response and good stability. Furthermore, uric acid (UA), ascorbic acid (AA) and dopamine (DA) had little interferences with the amperometric signal of H(2)O(2), which provide the perspective of this H(2)O(2) sensor to be used in biological environments. SN - 0956-5663 UR - https://www.unboundmedicine.com/medline/citation/16621505/Direct_electrochemistry_of_hemoglobin_in_PHEA_and_its_catalysis_to_H2O2_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0956-5663(06)00149-7 DB - PRIME DP - Unbound Medicine ER -