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Engineering of a novel chimera of superoxide dismutase and Vitreoscilla hemoglobin for rapid detoxification of reactive oxygen species

Isarankura-Na-Ayudhya, Chartchalerm; Yainoy, Sakda; Tantimongcolwat, Tanawut; Bülow, Leif LU and Prachayasittikul, Virapong (2010) In Journal of Bioscience and Bioengineering 110(6). p.633-637
Abstract
The genes encoding human manganese superoxide dismutase (MnSOD) and Vitreoscilla hemoglobin (VHb) were fused inframe to generate a bifunctional enzyme that possessed MnSOD and peroxidase-like activities. At neutral pH, the coupling of the SOD and peroxidase reactions revealed that the bifunctional enzyme exhibited a 2.5 times shorter transient period and a 1.67 times higher reaction rate at steady-state conditions. Furthermore, the catalytic rate of the bifunctional enzyme was not affected as much by the external H2O2 scavenger catalase. This indicates that the bifunctional protein possesses a greater antioxidant capability, which is possibly due to the close proximity between the active site of MnSOD and the heme moiety of VHb. Our... (More)
The genes encoding human manganese superoxide dismutase (MnSOD) and Vitreoscilla hemoglobin (VHb) were fused inframe to generate a bifunctional enzyme that possessed MnSOD and peroxidase-like activities. At neutral pH, the coupling of the SOD and peroxidase reactions revealed that the bifunctional enzyme exhibited a 2.5 times shorter transient period and a 1.67 times higher reaction rate at steady-state conditions. Furthermore, the catalytic rate of the bifunctional enzyme was not affected as much by the external H2O2 scavenger catalase. This indicates that the bifunctional protein possesses a greater antioxidant capability, which is possibly due to the close proximity between the active site of MnSOD and the heme moiety of VHb. Our findings not only provide insight into the synergistic functions of SOD and peroxidase but also could potentially be used to develop novel therapeutic agents with more efficient O-2 carrying capability. (C) 2010, The Society for Biotechnology, Japan. All rights reserved. (Less)
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author
organization
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Contribution to journal
publication status
published
subject
keywords
Bifunctional enzyme, Manganese superoxide dismutase, Vitreoscilla, hemoglobin, Reactive oxygen species, Sequential catalytic reactions
in
Journal of Bioscience and Bioengineering
volume
110
issue
6
pages
633 - 637
publisher
Elsevier
external identifiers
  • wos:000286701300002
  • scopus:78449264854
ISSN
1347-4421
DOI
10.1016/j.jbiosc.2010.07.001
language
English
LU publication?
yes
id
80db30bf-8e95-4b85-b23c-dcbf7429424b (old id 1868067)
date added to LUP
2011-04-20 08:28:16
date last changed
2018-05-29 10:26:16
@article{80db30bf-8e95-4b85-b23c-dcbf7429424b,
  abstract     = {The genes encoding human manganese superoxide dismutase (MnSOD) and Vitreoscilla hemoglobin (VHb) were fused inframe to generate a bifunctional enzyme that possessed MnSOD and peroxidase-like activities. At neutral pH, the coupling of the SOD and peroxidase reactions revealed that the bifunctional enzyme exhibited a 2.5 times shorter transient period and a 1.67 times higher reaction rate at steady-state conditions. Furthermore, the catalytic rate of the bifunctional enzyme was not affected as much by the external H2O2 scavenger catalase. This indicates that the bifunctional protein possesses a greater antioxidant capability, which is possibly due to the close proximity between the active site of MnSOD and the heme moiety of VHb. Our findings not only provide insight into the synergistic functions of SOD and peroxidase but also could potentially be used to develop novel therapeutic agents with more efficient O-2 carrying capability. (C) 2010, The Society for Biotechnology, Japan. All rights reserved.},
  author       = {Isarankura-Na-Ayudhya, Chartchalerm and Yainoy, Sakda and Tantimongcolwat, Tanawut and Bülow, Leif and Prachayasittikul, Virapong},
  issn         = {1347-4421},
  keyword      = {Bifunctional enzyme,Manganese superoxide dismutase,Vitreoscilla,hemoglobin,Reactive oxygen species,Sequential catalytic reactions},
  language     = {eng},
  number       = {6},
  pages        = {633--637},
  publisher    = {Elsevier},
  series       = {Journal of Bioscience and Bioengineering},
  title        = {Engineering of a novel chimera of superoxide dismutase and Vitreoscilla hemoglobin for rapid detoxification of reactive oxygen species},
  url          = {http://dx.doi.org/10.1016/j.jbiosc.2010.07.001},
  volume       = {110},
  year         = {2010},
}