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Author |
Trashin, S.; De Jong, M.; Luyckx, E.; Dewilde, S.; De Wael, K. |
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Title |
Electrochemical evidence for neuroglobin activity on NO at physiological concentrations |
Type |
A1 Journal article |
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Year  |
2016 |
Publication |
Journal of biological chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
291 |
Issue |
36 |
Pages |
18959-18966 |
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Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
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Abstract |
The true function of neuroglobin (Ngb) and, particularly, human Ngb (NGB) has been under debate since its discovery 15 years ago. It has been expected to play a role in oxygen binding/supply, but a variety of other functions have been put forward, including NO dioxygenase activity. However, in vitro studies that could unravel these potential roles have been hampered by the lack of an Ngb-specific reductase. In this work, we used electrochemical measurements to investigate the role of an intermittent internal disulfide bridge in determining NO oxidation kinetics at physiological NO concentrations. The use of a polarized electrode to efficiently interconvert the ferric (Fe3+) and ferrous (Fe2+) forms of an immobilized NGB showed that the disulfide bridge both defines the kinetics of NO dioxygenase activity and regulates appearance of the free ferrous deoxy-NGB, which is the redox active form of the protein in contrast to oxy-NGB. Our studies further identified a role for the distal histidine, interacting with the hexacoordinated iron atom of the heme, in oxidation kinetics. These findings may be relevant in vivo, for example in blocking apoptosis by reduction of ferric cytochrome c, and gentle tuning of NO concentration in the tissues. |
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Wos |
000383242300031 |
Publication Date |
2016-07-12 |
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ISSN |
0021-9258; 1083-351x |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
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Impact Factor |
4.125 |
Times cited |
11 |
Open Access |
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Notes |
; This work was supported by Fonds Wetenschappelijk Onderzoek (FWO) Grant G.0687.13 and Universiteit Antwerpen GOA BOF 28312. The authors declare that they have no conflicts of interest with the contents of this article. ; |
Approved |
Most recent IF: 4.125 |
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Call Number |
UA @ admin @ c:irua:134340 |
Serial |
5590 |
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Author |
De Henau, S.; Tilleman, L.; Vangheel, M.; Luyckx, E.; Trashin, S.; Pauwels, M.; Germani, F.; Vlaeminck, C.; Vanfleteren, J.R.; Bert, W.; Pesce, A.; Nardini, M.; Bolognesi, M.; De Wael, K.; Moens, L.; Dewilde, S.; Braeckman, B.P. |
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Title |
A redox signalling globin is essential for reproduction in Caenorhabditis elegans |
Type |
A1 Journal article |
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Year |
2015 |
Publication |
Nature communications |
Abbreviated Journal |
Nat Commun |
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Volume |
6 |
Issue |
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Pages |
8782 |
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Keywords |
A1 Journal article; Engineering sciences. Technology; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
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Abstract |
Moderate levels of reactive oxygen species (ROS) are now recognized as redox signalling molecules. However, thus far, only mitochondria and NADPH oxidases have been identified as cellular sources of ROS in signalling. Here we identify a globin (GLB-12) that produces superoxide, a type of ROS, which serves as an essential signal for reproduction in C. elegans. We find that GLB-12 has an important role in the regulation of multiple aspects in germline development, including germ cell apoptosis. We further describe how GLB-12 displays specific molecular, biochemical and structural properties that allow this globin to act as a superoxide generator. In addition, both an intra- and extracellular superoxide dismutase act as key partners of GLB-12 to create a transmembrane redox signal. Our results show that a globin can function as a driving factor in redox signalling, and how this signal is regulated at the subcellular level by multiple control layers. |
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Wos |
000367577100002 |
Publication Date |
2015-12-01 |
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Series Issue |
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Edition |
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ISSN |
2041-1723 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
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Impact Factor |
12.124 |
Times cited |
20 |
Open Access |
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Notes |
; We thank Dr K. Matsumoto and Dr T. Mizuno for kindly providing the mek-1(ks54) sek-1(km4) double mutant, the antibody anti-PMK-1 and technical advice on antibody use; Dr D. Kim for kindly providing the pDK177 RNAi strain; Dr M. Ubbink and Dr Q. Bashir for providing CCP; Dr K. Oegema and the OD lab for sharing technical expertise; M. Couvreur for assistance in generating transgenic lines; and Dr T. Dansen for the final support. Some strains were provided by the CGC, which is funded by the NIH Office of Research Infrastructure Programs (P40 OD010440). S.D.H. and F.G. are PhD fellows of the Fund for Scientific Research (FWO). Financial support to S.D. and L.M. was provided by the University of Antwerp (BOF UA TOP 2006), to K.D.W., S.D. and S.T. by the University of Antwerp (BOF-GOA) and to S.D., L.M., B.P.B., by FWO project G.0247.09. ; |
Approved |
Most recent IF: 12.124; 2015 IF: 11.470 |
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Call Number |
UA @ admin @ c:irua:129310 |
Serial |
5809 |
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