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Meszaros, Livia S.
Publications (5 of 5) Show all publications
Meszaros, L. S., Nemeth, B., Esmieu, C., Ceccaldi, P. & Berggren, G. (2018). InVivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases. Angewandte Chemie International Edition, 57(10), 2596-2599
Open this publication in new window or tab >>InVivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases
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2018 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 57, no 10, p. 2596-2599Article in journal (Refereed) Published
Abstract [en]

EPR spectroscopy reveals the formation of two different semi-synthetic hydrogenases invivo. [FeFe] hydrogenases are metalloenzymes that catalyze the interconversion of molecular hydrogen and protons. The reaction is catalyzed by the H-cluster, consisting of a canonical iron-sulfur cluster and an organometallic [2Fe] subsite. It was recently shown that the enzyme can be reconstituted with synthetic cofactors mimicking the composition of the [2Fe] subsite, resulting in semi-synthetic hydrogenases. Herein, we employ EPR spectroscopy to monitor the formation of two such semi-synthetic enzymes in whole cells. The study provides the first spectroscopic characterization of semi-synthetic hydrogenases invivo, and the observation of two different oxidized states of the H-cluster under intracellular conditions. Moreover, these findings underscore how synthetic chemistry can be a powerful tool for manipulation and examination of the hydrogenase enzyme under invivo conditions.

Place, publisher, year, edition, pages
WILEY-V C H VERLAG GMBH, 2018
Keywords
[FeFe] hydrogenase, artificial enzymes, EPR spectroscopy, metalloenzymes
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:uu:diva-348975 (URN)10.1002/anie.201710740 (DOI)000426252400010 ()29334424 (PubMedID)
Funder
Swedish Research Council, 21-2014-5670Swedish Research Council for Environment, Agricultural Sciences and Spatial Planning, 213-2014-880EU, European Research Council, 714102
Available from: 2018-05-03 Created: 2018-05-03 Last updated: 2019-09-18Bibliographically approved
Magnuson, A., Raleiras, P., Meszaros, L. S., Khanna, N., Miranda, H., Ho, F. M., . . . Styring, S. (2018). Sustainable photobiological hydrogen production via protein engineering of cyanobacterial hydrogenases. Paper presented at 255th National Meeting and Exposition of the American-Chemical-Society (ACS) - Nexus of Food, Energy, and Water, MAR 18-22, 2018, New Orleans, USA.. Abstract of Papers of the American Chemical Society, 255
Open this publication in new window or tab >>Sustainable photobiological hydrogen production via protein engineering of cyanobacterial hydrogenases
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2018 (English)In: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 255Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
Washington, D.C.: American Chemical Society (ACS), 2018
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:uu:diva-368928 (URN)000435539900440 ()
Conference
255th National Meeting and Exposition of the American-Chemical-Society (ACS) - Nexus of Food, Energy, and Water, MAR 18-22, 2018, New Orleans, USA.
Note

Meeting Abstract: 443

Available from: 2018-12-11 Created: 2018-12-11 Last updated: 2018-12-11Bibliographically approved
Khanna, N., Esmieu, C., Meszaros, L. S., Lindblad, P. & Berggren, G. (2017). In vivo activation of an [FeFe] hydrogenase using synthetic cofactors. Energy & Environmental Science, 10(7), 1563-1567
Open this publication in new window or tab >>In vivo activation of an [FeFe] hydrogenase using synthetic cofactors
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2017 (English)In: Energy & Environmental Science, ISSN 1754-5692, E-ISSN 1754-5706, Vol. 10, no 7, p. 1563-1567Article in journal (Refereed) Published
Abstract [en]

[FeFe] hydrogenases catalyze the reduction of protons, and oxidation of hydrogen gas, with remarkable efficiency. The reaction occurs at the H-cluster, which contains an organometallic [2Fe] subsite. The unique nature of the [2Fe] subsite makes it dependent on a specific set of maturation enzymes for its biosynthesis and incorporation into the apo-enzyme. Herein we report on how this can be circumvented, and the apo-enzyme activated in vivo by synthetic active site analogues taken up by the living cell.

National Category
Chemical Sciences
Identifiers
urn:nbn:se:uu:diva-330015 (URN)10.1039/c7ee00135e (DOI)000405279900003 ()
Funder
Swedish Research Council, 621-2014-5670Swedish Research Council Formas, 213-2014-880Swedish Energy Agency, 11674-5Knut and Alice Wallenberg Foundation, 2011.0067Wenner-Gren Foundations
Note

Correction in: ENERGY & ENVIRONMENTAL SCIENCE, Volume: 11, Issue: 11, Pages: 3321-3321, DOI: 10.1039/c8ee90054j

Available from: 2017-10-11 Created: 2017-10-11 Last updated: 2019-01-17Bibliographically approved
Kovacs, D., Lu, X., Meszaros, L. S., Ott, M., Andres, J. & Borbas, K. E. (2017). Photophysics of Coumarin and Carbostyril-Sensitized Luminescent Lanthanide Complexes: Implications for Complex Design in Multiplex Detection. Journal of the American Chemical Society, 139(16), 5756-5767
Open this publication in new window or tab >>Photophysics of Coumarin and Carbostyril-Sensitized Luminescent Lanthanide Complexes: Implications for Complex Design in Multiplex Detection
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2017 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 139, no 16, p. 5756-5767Article in journal (Refereed) Published
Abstract [en]

Luminescent lanthanide (Ln(III)) complexes with coumarin or carbostyril antennae were synthesized and their photophysical properties evaluated using steady-state and time-resolved UV-vis spectroscopy. Ligands bearing distant hydroxycoumarin-derived antennae attached through triazole linkers were modest sensitizers for Eu(III) and Tb(III), whereas ligands with 7-amidocarbostyrils directly linked to the coordination site could reach good quantum yields for multiple Ln(III), including the visible emitters Sm(III) and Dy(III), and the near-infrared emitters Nd(III) and Yb(III). The highest lanthanide-centered luminescence quantum yields were 35% (Tb), 7.9% (Eu), 0.67% (Dy), and 0.18% (Sm). Antennae providing similar luminescence intensities with 2-4 Ln-emitters were identified. Photoredox quenching of the carbostyril antenna excited states was observed for all Eu(III)-complexes and should be sensitizing in the case of Yb(III); the scope of the process extends to Ln(III) for which it has not been seen previously, specifically Dy(III) and Sm(III). The proposed process is supported by photophysical and electrochemical data. A FRET-type mechanism was identified in architectures with both distant and close antennae for all of the Lns. This mechanism seems to be the only sensitizing one at long distance and probably contributes to the sensitization at shorter distances along with the triplet pathway. The complexes were nontoxic to either bacterial or mammalian cells. Complexes of an ester-functionalized ligand were taken up by bacteria in a concentration-dependent manner. Our results suggest that the effects of FRET and photoredox quenching should be taken into consideration when designing luminescent Ln complexes. These results also establish these Ln(III)-complexes for multiplex detection beyond the available two-color systems.

Place, publisher, year, edition, pages
AMER CHEMICAL SOC, 2017
National Category
Chemical Sciences Engineering and Technology
Identifiers
urn:nbn:se:uu:diva-322722 (URN)10.1021/jacs.6b11274 (DOI)000400321500029 ()28388066 (PubMedID)
Funder
Swedish Research Council, 2013-4655Stiftelsen Olle Engkvist Byggmästare
Available from: 2017-05-29 Created: 2017-05-29 Last updated: 2019-04-16Bibliographically approved
Raleiras, P., Khanna, N., Miranda, H., Meszaros, L. S., Krassen, H., Ho, F., . . . Styring, S. (2016). Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme. Energy & Environmental Science, 9(2), 581-594
Open this publication in new window or tab >>Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme
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2016 (English)In: Energy & Environmental Science, ISSN 1754-5692, E-ISSN 1754-5706, Vol. 9, no 2, p. 581-594Article in journal (Refereed) Published
Abstract [en]

The filamentous cyanobacterium Nostoc punctiforme ATCC 29133 produces hydrogen via nitrogenase in heterocysts upon onset of nitrogen-fixing conditions. N. punctiforme expresses concomitantly the uptake hydrogenase HupSL, which oxidizes hydrogen in an effort to recover some of the reducing power used up by nitrogenase. Eliminating uptake activity has been employed as a strategy for net hydrogen production in N. punctiforme (Lindberg et al., Int. J. Hydrogen Energy, 2002, 27, 1291-1296). However, nitrogenase activity wanes within a few days. In the present work, we modify the proximal iron-sulfur cluster in the hydrogenase small subunit HupS by introducing the designed mutation C12P in the fusion protein f-HupS for expression in E. coli (Raleiras et al., J. Biol. Chem., 2013, 288, 18345-18352), and in the full HupSL enzyme for expression in N. punctiforme. C12P f-HupS was investigated by EPR spectroscopy and found to form a new paramagnetic species at the proximal cluster site consistent with a [4Fe-4S] to [3Fe-4S] cluster conversion. The new cluster has the features of an unprecedented mixed-coordination [3Fe-4S] metal center. The mutation was found to produce stable protein in vitro, in silico and in vivo. When C12P HupSL was expressed in N. punctiforme, the strain had a consistently higher hydrogen production than the background [capital Delta]hupSL mutant. We conclude that the increase in hydrogen production is due to the modification of the proximal iron-sulfur cluster in HupS, leading to a turn of the electron flow in the enzyme.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2016
National Category
Chemical Sciences
Identifiers
urn:nbn:se:uu:diva-271302 (URN)10.1039/C5EE02694F (DOI)000369744500023 ()
Funder
Knut and Alice Wallenberg Foundation, 2011.0067EU, FP7, Seventh Framework Programme, 317184Swedish Energy Agency, 11674-5
Available from: 2016-01-07 Created: 2016-01-07 Last updated: 2017-12-01Bibliographically approved
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