Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin
Xin Gan, Tao Liu, Jun Zhong, Xinjian Liu, Genxi Li
Laboratory Medicine and Pathology
Silver nanoparticles (11 ± 1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Direct fast electron transfer between Mb and a pyrolytic graphite (PG) electrode was achieved, and a pair of well-defined, quasireversible redox peaks was obtained. The cathodic and anodic peaks were located at -329 and -281 mV, respectively. Meanwhile, the catalytic ability of the protein toward the reduction of H2O2 was also studied, and a H2O2 biosensor was subsequently fabricated. Its detection limit was 1.0 × 10-6M with a sensitivity of 0.0205 μA per μM of H2O2. The apparent Michaelis-Menten constant was calculated to be 1303 μM. Flocculation assay showed that the protein maintained plasmon layers surrounding the surface of silver nanoparticles and avoided silver-nanopartkle aggregation. On the other hand, UV-visible spectroscopy studies revealed that silver nanoparticles could induce a small change of the heme-group environment of the protein; this contributed to the enhancement of the electron-transfer reactivity and the catalytic activity.
ChemBioChem
https://doi.org/10.1002/cbic.200400080
Myoglobin
10.1002/cbic.200400080
Gan, X., Liu, T., Zhong, J., Liu, X., & Li, G. (2004). Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin. ChemBioChem, 5(12), 1686-1691. https://doi.org/10.1002/cbic.200400080
Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin. / Gan, Xin; Liu, Tao; Zhong, Jun; Liu, Xinjian; Li, Genxi.
In: ChemBioChem, Vol. 5, No. 12, 2004, p. 1686-1691.
Gan, X, Liu, T, Zhong, J, Liu, X & Li, G 2004, 'Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin', ChemBioChem, vol. 5, no. 12, pp. 1686-1691. https://doi.org/10.1002/cbic.200400080
Gan X, Liu T, Zhong J, Liu X, Li G. Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin. ChemBioChem. 2004;5(12):1686-1691. https://doi.org/10.1002/cbic.200400080
Gan, Xin ; Liu, Tao ; Zhong, Jun ; Liu, Xinjian ; Li, Genxi. / Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin. In: ChemBioChem. 2004 ; Vol. 5, No. 12. pp. 1686-1691.
@article{91a6685b69e84e91955478cb593f138d,
title = "Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin",
abstract = "Silver nanoparticles (11 ± 1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Direct fast electron transfer between Mb and a pyrolytic graphite (PG) electrode was achieved, and a pair of well-defined, quasireversible redox peaks was obtained. The cathodic and anodic peaks were located at -329 and -281 mV, respectively. Meanwhile, the catalytic ability of the protein toward the reduction of H2O2 was also studied, and a H2O2 biosensor was subsequently fabricated. Its detection limit was 1.0 × 10-6M with a sensitivity of 0.0205 μA per μM of H2O2. The apparent Michaelis-Menten constant was calculated to be 1303 μM. Flocculation assay showed that the protein maintained plasmon layers surrounding the surface of silver nanoparticles and avoided silver-nanopartkle aggregation. On the other hand, UV-visible spectroscopy studies revealed that silver nanoparticles could induce a small change of the heme-group environment of the protein; this contributed to the enhancement of the electron-transfer reactivity and the catalytic activity.",
keywords = "Electrochemistry, Electrodes, Myoglobin, Nanoparticles, Silver",
author = "Xin Gan and Tao Liu and Jun Zhong and Xinjian Liu and Genxi Li",
doi = "10.1002/cbic.200400080",
journal = "ChemBioChem",
publisher = "Wiley-VCH Verlag",
T1 - Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin
AU - Gan, Xin
AU - Liu, Tao
AU - Zhong, Jun
AU - Liu, Xinjian
AU - Li, Genxi
N2 - Silver nanoparticles (11 ± 1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Direct fast electron transfer between Mb and a pyrolytic graphite (PG) electrode was achieved, and a pair of well-defined, quasireversible redox peaks was obtained. The cathodic and anodic peaks were located at -329 and -281 mV, respectively. Meanwhile, the catalytic ability of the protein toward the reduction of H2O2 was also studied, and a H2O2 biosensor was subsequently fabricated. Its detection limit was 1.0 × 10-6M with a sensitivity of 0.0205 μA per μM of H2O2. The apparent Michaelis-Menten constant was calculated to be 1303 μM. Flocculation assay showed that the protein maintained plasmon layers surrounding the surface of silver nanoparticles and avoided silver-nanopartkle aggregation. On the other hand, UV-visible spectroscopy studies revealed that silver nanoparticles could induce a small change of the heme-group environment of the protein; this contributed to the enhancement of the electron-transfer reactivity and the catalytic activity.
AB - Silver nanoparticles (11 ± 1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Direct fast electron transfer between Mb and a pyrolytic graphite (PG) electrode was achieved, and a pair of well-defined, quasireversible redox peaks was obtained. The cathodic and anodic peaks were located at -329 and -281 mV, respectively. Meanwhile, the catalytic ability of the protein toward the reduction of H2O2 was also studied, and a H2O2 biosensor was subsequently fabricated. Its detection limit was 1.0 × 10-6M with a sensitivity of 0.0205 μA per μM of H2O2. The apparent Michaelis-Menten constant was calculated to be 1303 μM. Flocculation assay showed that the protein maintained plasmon layers surrounding the surface of silver nanoparticles and avoided silver-nanopartkle aggregation. On the other hand, UV-visible spectroscopy studies revealed that silver nanoparticles could induce a small change of the heme-group environment of the protein; this contributed to the enhancement of the electron-transfer reactivity and the catalytic activity.
KW - Electrochemistry
KW - Electrodes
KW - Myoglobin
KW - Nanoparticles
KW - Silver
U2 - 10.1002/cbic.200400080
DO - 10.1002/cbic.200400080
JO - ChemBioChem
JF - ChemBioChem