TY - JOUR
T1 - Liposome membrane can act like molecular and metal chaperones for oxidized and fragmented superoxide dismutase
AU - Tuan, Le Quoc
AU - Umakoshi, Hiroshi
AU - Shimanouchi, Toshinori
AU - Kuboi, Ryoichi
N1 - Funding Information:
The fundamental concept of this study was supported by the research group of Membrane Stress Biotechnology. The study was partially supported by a Grant-in-Aid for Scientific Research (nos. 15206089, 16686046, 16760635, 17656268, 19656203, 19656220, and 20360350) from the Ministry of Education, Science, Sports, and Culture of Japan, and a grant from the 21st Century COE program “Creation of Integrated EcoChemistry” and Global COE program “Bio-Environmental Chemistry” of the Japan Society for the Promotion of Science (JSPS). We are grateful to the Research Center for Solar Energy Chemistry of Osaka University and the Gas Hydrate Analyzing System of Osaka University. L.Q. Tuan also acknowledges financial support from the Ministry of Education and Training in Vietnam (MOET).
PY - 2009/2/5
Y1 - 2009/2/5
N2 - A mechanism for liposome-recruited activity of oxidized and fragmented superoxide dismutase (Fr.-SOD) [Tuan LQ, Umakoshi H, Shimanouchi T, Kuboi R. Liposome-recruited activity of oxidized and fragmented superoxide dismutase. Langmuir 2008;24:350-4] was further investigated, focusing on the secondary structure of Fr.-SOD. Liposome membrane was found to assist the conformational change of Fr.-SOD and reactivate the enzymatic activity, like molecular and metal chaperones. The loss of SOD activity and its secondary structure was observed during 6 h oxidation in 2 mM hydrogen peroxide. The contents of the α-helix and β-sheet structures in the oxidized and fragmented SOD (2 μM) were increased only in the presence of 10 μM Cu2+ and Zn2+ together, or in the presence of 2 mM POPC liposomes. The mixture of all of these elements (fragmented SOD and POPC liposomes with Cu2+ and Zn2+) gave not only the increase of the α-helix and β-sheet contents but also the mediation of the high SOD-like activity.
AB - A mechanism for liposome-recruited activity of oxidized and fragmented superoxide dismutase (Fr.-SOD) [Tuan LQ, Umakoshi H, Shimanouchi T, Kuboi R. Liposome-recruited activity of oxidized and fragmented superoxide dismutase. Langmuir 2008;24:350-4] was further investigated, focusing on the secondary structure of Fr.-SOD. Liposome membrane was found to assist the conformational change of Fr.-SOD and reactivate the enzymatic activity, like molecular and metal chaperones. The loss of SOD activity and its secondary structure was observed during 6 h oxidation in 2 mM hydrogen peroxide. The contents of the α-helix and β-sheet structures in the oxidized and fragmented SOD (2 μM) were increased only in the presence of 10 μM Cu2+ and Zn2+ together, or in the presence of 2 mM POPC liposomes. The mixture of all of these elements (fragmented SOD and POPC liposomes with Cu2+ and Zn2+) gave not only the increase of the α-helix and β-sheet contents but also the mediation of the high SOD-like activity.
KW - Chaperones
KW - Enzymatic activity
KW - Hydrogen peroxide
KW - Liposomes
KW - Superoxide dismutase
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U2 - 10.1016/j.enzmictec.2008.10.012
DO - 10.1016/j.enzmictec.2008.10.012
M3 - Article
AN - SCOPUS:57549085702
SN - 0141-0229
VL - 44
SP - 101
EP - 106
JO - Enzyme and Microbial Technology
JF - Enzyme and Microbial Technology
IS - 2
ER -