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Publications (10 of 32) Show all publications
Grinberg, I. R., Lundin, D., Sahlin, M., Crona, M., Berggren, G., Hofer, A. & Sjoberg, B.-M. (2018). A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant. Journal of Biological Chemistry, 293(41), 15889-15900
Open this publication in new window or tab >>A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant
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2018 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 293, no 41, p. 15889-15900Article in journal (Refereed) Published
Abstract [en]

Class I ribonucleotide reductase (RNR) consists of a catalytic subunit (NrdA) and a radical-generating subunit (NrdB) that together catalyze reduction of ribonucleotides to their corresponding deoxyribonucleotides. NrdB from the firmicute Facklamia ignava is a unique fusion protein with N-terminal addons of a glutaredoxin (Grx) domain followed by an ATP-binding domain, the ATP cone. Grx, usually encoded separately from the RNR operon, is a known RNR reductant. We show that the fused Grx domain functions as an efficient reductant of the F. ignava class I RNR via the common dithiol mechanism and, interestingly, also via a monothiol mechanism, although less efficiently. To our knowledge, a Grx that uses both of these two reaction mechanisms has not previously been observed with a native substrate. The ATP cone is in most RNRs an N-terminal domain of the catalytic subunit. It is an allosteric on/off switch promoting ribonucleotide reduction in the presence of ATP and inhibiting RNR activity in the presence of dATP. We found that dATP bound to the ATP cone of F. ignava NrdB promotes formation of tetramers that cannot form active complexes with NrdA. The ATP cone bound two dATP molecules but only one ATP molecule. F. ignava NrdB contains the recently identified radical-generating cofactor Mn-III/Mn-IV. We show that NrdA from F. ignava can form a catalytically competent RNR with the Mn-III/Mn-IV-containing NrdB from the flavobacterium Leeuwenhoekiella blandensis. In conclusion, F. ignava NrdB is fused with a Grx functioning as an RNR reductant and an ATP cone serving as an on/off switch.

Place, publisher, year, edition, pages
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2018
Keywords
ribonucleotide reductase, allosteric regulation, oxidation-reduction (redox), radical, manganese, ATP-cone, dATP inhibition, dithiol-monothiol, glutaredoxin, tetramers
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:uu:diva-369105 (URN)10.1074/jbc.RA118.004991 (DOI)000447256000013 ()30166338 (PubMedID)
Funder
Swedish Research Council, 2016-01920Swedish Research Council, 621-2014-5670Swedish Research Council Formas, 213-2014-880EU, European Research Council, 714102Swedish Cancer Society, CAN 2016/670Carl Tryggers foundation The Wenner-Gren Foundation
Available from: 2018-12-17 Created: 2018-12-17 Last updated: 2018-12-17Bibliographically approved
Esmieu, C., Raleiras, P. & Berggren, G. (2018). From protein engineering to artificial enzymes - biological and biomimetic approaches towards sustainable hydrogen production. SUSTAINABLE ENERGY & FUELS, 2(4), 724-750
Open this publication in new window or tab >>From protein engineering to artificial enzymes - biological and biomimetic approaches towards sustainable hydrogen production
2018 (English)In: SUSTAINABLE ENERGY & FUELS, ISSN 2398-4902, Vol. 2, no 4, p. 724-750Article, review/survey (Refereed) Published
Abstract [en]

Hydrogen gas is used extensively in industry today and is often put forward as a suitable energy carrier due its high energy density. Currently, the main source of molecular hydrogen is fossil fuels via steam reforming. Consequently, novel production methods are required to improve the sustainability of hydrogen gas for industrial processes, as well as paving the way for its implementation as a future solar fuel. Nature has already developed an elaborate hydrogen economy, where the production and consumption of hydrogen gas is catalysed by hydrogenase enzymes. In this review we summarize efforts on engineering and optimizing these enzymes for biological hydrogen gas production, with an emphasis on their inorganic cofactors. Moreover, we will describe how our understanding of these enzymes has been applied for the preparation of bio-inspired/-mimetic systems for efficient and sustainable hydrogen production.

Place, publisher, year, edition, pages
ROYAL SOC CHEMISTRY, 2018
National Category
Chemical Sciences
Identifiers
urn:nbn:se:uu:diva-357183 (URN)10.1039/c7se00582b (DOI)000428778800002 ()
Funder
Swedish Research Council, 621-2014-5670Swedish Research Council Formas, 213-2014-880EU, European Research Council, 714102
Available from: 2018-08-13 Created: 2018-08-13 Last updated: 2018-08-13Bibliographically approved
Wegelius, A., Khanna, N., Esmieu, C., Barone, G. D., Pinto, F., Tamagnini, P., . . . Lindblad, P. (2018). Generation of a functional, semisynthetic [FeFe]-hydrogenase in a photosynthetic microorganism. Energy & Environmental Science, 11(11), 3163-3167
Open this publication in new window or tab >>Generation of a functional, semisynthetic [FeFe]-hydrogenase in a photosynthetic microorganism
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2018 (English)In: Energy & Environmental Science, ISSN 1754-5692, E-ISSN 1754-5706, Vol. 11, no 11, p. 3163-3167Article in journal (Refereed) Published
Abstract [en]

[FeFe]-Hydrogenases are hydrogen producing metalloenzymes with excellent catalytic capacities, highly relevant in the context of a future hydrogen economy. Here we demonstrate the synthetic activation of a heterologously expressed [FeFe]-hydrogenase in living cells of Synechocystis PCC 6803, a photoautotrophic microbial chassis with high potential for biotechnological energy applications. H-2-Evolution assays clearly show that the non-native, semi-synthetic enzyme links to the native metabolism in living cells.

National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:uu:diva-371404 (URN)10.1039/c8ee01975d (DOI)000449843300006 ()
Funder
EU, European Research Council, 714102Swedish Energy Agency, 11674-5Knut and Alice Wallenberg Foundation, 2011.0067Wenner-Gren FoundationsNordForsk, 82845
Note

Adam Wegelius and Namita Khanna contributed equally to this work.

Available from: 2018-12-20 Created: 2018-12-20 Last updated: 2019-01-07Bibliographically approved
Tian, H., Nemeth, B., Berggren, G. & Tian, L. (2018). Hydrogen evolution by a photoelectrochemical cell based on a Cu2O-ZnO-[FeFe] hydrogenase electrode. Journal of Photochemistry and Photobiology A: Chemistry, 366, 27-33
Open this publication in new window or tab >>Hydrogen evolution by a photoelectrochemical cell based on a Cu2O-ZnO-[FeFe] hydrogenase electrode
2018 (English)In: Journal of Photochemistry and Photobiology A: Chemistry, ISSN 1010-6030, E-ISSN 1873-2666, Vol. 366, p. 27-33Article in journal (Refereed) Published
Abstract [en]

A Cu2O-ZnO-hydrogenase photocathode possessed enzyme/semiconductor junction has been constructed by immobilizing a biological protein catalyst, hydrogenase-CrHydA1 enzyme on the ZnO protected Cu2O electrode. With light illumination, a photocurrent of 0.8 mA/cm2 at 0.15 V vs. RHE was obtained and hydrogen was successfully detected from the photocathode in photoelectrochemical measurements with Faradaic efficiency of ca. 1%. The construction as well as the stability of the system are also reported. The result shows that this biohybrid photocathode is capable of photocatalytic proton reduction under mild conditions.

National Category
Chemical Sciences
Identifiers
urn:nbn:se:uu:diva-371529 (URN)10.1016/j.jphotochem.2018.01.035 (DOI)000452577600005 ()
Funder
Stiftelsen Olle Engkvist Byggmästare, 2015/456J. Gust. Richert stiftelse, 2016-00231Swedish Energy Agency, 111674-8Swedish Research Council, 621-2014-5670Swedish Research Council Formas, 213-2014-880Wenner-Gren Foundations
Available from: 2018-12-21 Created: 2018-12-21 Last updated: 2019-01-16Bibliographically approved
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: 2018-05-03Bibliographically approved
Schuth, N., Zaharieva, I., Chernev, P., Berggren, G., Anderlund, M., Styring, S., . . . Haumann, M. (2018). K alpha X-ray Emission Spectroscopy on the Photosynthetic Oxygen-Evolving Complex Supports Manganese Oxidation and Water Binding in the S-3 State. Inorganic Chemistry, 57(16), 10424-10430
Open this publication in new window or tab >>K alpha X-ray Emission Spectroscopy on the Photosynthetic Oxygen-Evolving Complex Supports Manganese Oxidation and Water Binding in the S-3 State
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2018 (English)In: Inorganic Chemistry, ISSN 0020-1669, E-ISSN 1520-510X, Vol. 57, no 16, p. 10424-10430Article in journal (Refereed) Published
Abstract [en]

The unique manganese calcium-catalyst in photosystem II (PSII) is the natural paragon for efficient light driven water oxidation to yield O-2. The oxygen-evolving complex (OEC) in the dark-stable state (S-1) comprises a Mn4CaO4 core with five metal-bound water species. Binding and modification of the water molecules that are substrates of the water-oxidation reaction is mechanistically crucial but controversially debated. Two recent crystal structures of the OEC in its highest oxidation state (S-3) show either a vacant Mn coordination site or a bound peroxide species. For purified PSII at room temperature, we collected Mn K alpha X-ray emission spectra of the S-0, S-1, S-2, and S-3 intermediates in the OEC cycle, which were analyzed by comparison to synthetic Mn compounds, spectral simulations, and OEC models from density functional theory. Our results contrast both crystallographic structures. They indicate Mn oxidation in three S-transitions and suggest additional water binding at a previously open Mn coordination site. These findings exclude Mn reduction and render peroxide formation in S-3 unlikely.

Place, publisher, year, edition, pages
AMER CHEMICAL SOC, 2018
National Category
Inorganic Chemistry
Identifiers
urn:nbn:se:uu:diva-364392 (URN)10.1021/acs.inorgchem.8b01674 (DOI)000442489100090 ()30067343 (PubMedID)
Funder
Swedish Energy AgencyKnut and Alice Wallenberg Foundation
Available from: 2018-11-02 Created: 2018-11-02 Last updated: 2018-11-02Bibliographically approved
Berggren, G., Sjöberg, B.-M. & Lundin, D. (2018). Metalloprotein active site assembly: Assembly of homometallic and heterometallic Mn clusters. In: Metalloprotein Active Site Assembly: . John Wiley & Sons
Open this publication in new window or tab >>Metalloprotein active site assembly: Assembly of homometallic and heterometallic Mn clusters
2018 (English)In: Metalloprotein Active Site Assembly, John Wiley & Sons, 2018Chapter in book (Refereed)
Place, publisher, year, edition, pages
John Wiley & Sons, 2018
National Category
Chemical Sciences Biological Sciences
Identifiers
urn:nbn:se:uu:diva-371556 (URN)
Available from: 2018-12-21 Created: 2018-12-21 Last updated: 2018-12-21
Grinberg, I. R., Lundin, D., Hasan, M., Crona, M., Jonna, V. R., Loderer, C., . . . Sjöberg, B.-M. (2018). Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit. eLIFE, 7, Article ID e31529.
Open this publication in new window or tab >>Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit
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2018 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 7, article id e31529Article in journal (Refereed) Published
Abstract [en]

Ribonucleotide reductases (RNRs) are key enzymes in DNA metabolism, with allosteric mechanisms controlling substrate specificity and overall activity. In RNRs, the activity master-switch, the ATP-cone, has been found exclusively in the catalytic subunit. In two class I RNR subclasses whose catalytic subunit lacks the ATP-cone, we discovered ATP-cones in the radical-generating subunit. The ATP-cone in the Leeuwenhoekiella blandensis radical-generating subunit regulates activity via quaternary structure induced by binding of nucleotides. ATP induces enzymatically competent dimers, whereas dATP induces non-productive tetramers, resulting in different holoenzymes. The tetramer forms by interactions between ATP-cones, shown by a 2.45 A crystal structure. We also present evidence for an (MnMnIV)-Mn-III metal center. In summary, lack of an ATP-cone domain in the catalytic subunit was compensated by transfer of the domain to the radical-generating subunit. To our knowledge, this represents the first observation of transfer of an allosteric domain between components of the same enzyme complex.

Place, publisher, year, edition, pages
ELIFE SCIENCES PUBLICATIONS LTD, 2018
National Category
Biological Sciences
Identifiers
urn:nbn:se:uu:diva-345724 (URN)10.7554/eLife.31529 (DOI)000423786200001 ()
Funder
Swedish Cancer Society, CAN 721 2016/670Swedish Research Council, 2016-01920, 2016-04855, 621-2014-5670Wenner-Gren FoundationsCarl Tryggers foundation Swedish Research Council Formas, 213-2014-880EU, Horizon 2020, 714102
Available from: 2018-03-14 Created: 2018-03-14 Last updated: 2018-03-14Bibliographically 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
Esmieu, C. & Berggren, G. (2016). Characterization of a monocyanide model of FeFe hydrogenases - highlighting the importance of the bridgehead nitrogen for catalysis. Dalton Transactions, 45(48), 19242-19248
Open this publication in new window or tab >>Characterization of a monocyanide model of FeFe hydrogenases - highlighting the importance of the bridgehead nitrogen for catalysis
2016 (English)In: Dalton Transactions, ISSN 1477-9226, E-ISSN 1477-9234, Vol. 45, no 48, p. 19242-19248Article in journal (Refereed) Published
Abstract [en]

An azadithiolate bridged monocyanide derivative [Fe-2(adt)(CO)(5)(CN)](-) of [Fe-2(adt)(CO)(4)(CN)(2)](2-) has been prepared and extensively characterized as a model of the [FeFe]-hydrogenase active site, using a combination of FTIR spectroscopy, electrochemical methods and catalytic assays with chemical reductants. The presence of two basic nitrogen sites opens up multiple protonation pathways, enabling catalytic proton reduction. To our knowledge [Fe-2(adt)(CO)(5)(CN)](-) represents the first example of a cyanide containing [FeFe]-hydrogenase active site mimic capable of catalytic H-2 formation in aqueous media.

National Category
Inorganic Chemistry
Identifiers
urn:nbn:se:uu:diva-314063 (URN)10.1039/c6dt02061e (DOI)000390470400010 ()27549900 (PubMedID)
Funder
Swedish Research Council, 621-2014-5670Swedish Research Council Formas, 213-2014-880Wenner-Gren Foundations
Available from: 2017-01-26 Created: 2017-01-26 Last updated: 2017-11-29Bibliographically approved
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ORCID iD: ORCID iD iconorcid.org/0000-0002-6717-6612

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