Engineering of a novel chimera of superoxide dismutase and Vitreoscilla hemoglobin for rapid detoxification of reactive oxygen species
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1868067
- author
- Isarankura-Na-Ayudhya, Chartchalerm ; Yainoy, Sakda ; Tantimongcolwat, Tanawut ; Bülow, Leif LU and Prachayasittikul, Virapong
- organization
- publishing date
- 2010
- type
- 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
- pmid:20656555
- 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
- 2016-04-01 10:57:44
- date last changed
- 2022-02-10 07:40:23
@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}},
keywords = {{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}},
doi = {{10.1016/j.jbiosc.2010.07.001}},
volume = {{110}},
year = {{2010}},
}