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Publications (10 of 25) 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: 2018-05-03Bibliographically approved
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
Available from: 2017-10-11 Created: 2017-10-11 Last updated: 2017-10-11Bibliographically 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
Roy, S., Bacchi, M., Berggren, G. & Artero, V. (2015). A Systematic Comparative Study of Hydrogen-Evolving Molecular Catalysts in Aqueous Solutions. ChemSusChem, 8(21), 3632-3638
Open this publication in new window or tab >>A Systematic Comparative Study of Hydrogen-Evolving Molecular Catalysts in Aqueous Solutions
2015 (English)In: ChemSusChem, ISSN 1864-5631, E-ISSN 1864-564X, Vol. 8, no 21, p. 3632-3638Article in journal (Refereed) Published
Abstract [en]

We describe here a systematic, reliable, and fast screening method that allows the comparison of H-2-forming catalysts that work under aqueous conditions with two readily prepared chemical reductants and two commonly used photosensitizers. This method uses a Clark-type microsensor for H-2 detection and complements previous methods based on rotating disk electrode measurements. The efficiencies of a series of H-2-producing catalysts based on Co, Ni, Fe, and Pt were investigated in aqueous solutions under thermal conditions with europium(II) reductants and under photochemical conditions in the presence of two different photosensitizers {[Ru(bipy)(3)]Cl-2 (bipy=2,2-bipyridine) and eosin-Y} and sacrificial electron donors (ascorbate and triethanolamine, respectively). The majority of catalysts tested were active only under specific conditions. However, our results also demonstrate the impressive versatility of a group of Co catalysts, which were able to produce H-2 under different reducing conditions and at various pH values. In particular, a cobaloxime, [Co(dmgH)(2)(H2O)(2)] (dmgH(2)=dimethylglyoxime), and a cobalt tetraazamacrocyclic complex, {Co(CR)Cl-2}(+) [CR=2,12-dimethyl-3,7,11,17-tetraazabicylo(11.3.1)heptadeca-1(17),2,11,13,15-pentaene], displayed excellent catalytic rates under the studied conditions, and the best rates were observed under thermal conditions.

Keywords
analytical methods, electrochemistry, homogeneous catalysis, hydrogen evolution reaction, photochemistry
National Category
Chemical Sciences
Identifiers
urn:nbn:se:uu:diva-268779 (URN)10.1002/cssc.201501002 (DOI)000364525800013 ()26383700 (PubMedID)
Funder
Swedish Research Council Formas, 213-2014-880Swedish Research Council, 621-2014-5670Magnus Bergvall Foundation
Available from: 2015-12-15 Created: 2015-12-09 Last updated: 2017-12-01Bibliographically approved
Artero, V., Berggren, G., Atta, M., Caserta, G., Roy, S., Pecqueur, L. & Fontecave, M. (2015). From Enzyme Maturation to Synthetic Chemistry: The Case of Hydrogenases. Accounts of Chemical Research, 48(8), 2380-2387
Open this publication in new window or tab >>From Enzyme Maturation to Synthetic Chemistry: The Case of Hydrogenases
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2015 (English)In: Accounts of Chemical Research, ISSN 0001-4842, E-ISSN 1520-4898, Vol. 48, no 8, p. 2380-2387Article, review/survey (Refereed) Published
Abstract [en]

CONSPECTUS: Water splitting into oxygen and hydrogen is one of the most attractive strategies for storing solar energy and electricity. Because the processes at work are multielectronic, there is a crucial need for efficient and stable catalysts, which in addition have to be cheap for future industrial developments (electrolyzers, photoelectrochemicals, and fuel cells). Specifically for the water/hydrogen interconversion, Nature is an exquisite source of inspiration since this chemistry contributes to the bioenergetic metabolism of a number of living organisms via the activity of fascinating metalloenzymes, the hydrogenases. In this Account, we first briefly describe the structure of the unique dinuclear organometallic active sites of the two classes of hydrogenases as well as the complex protein machineries involved in their biosynthesis, their so-called maturation processes. This knowledge allows for the development of a fruitful bioinspired chemistry approach, which has already led to a number of interesting and original catalysts mimicking the natural active sites. More specifically, we describe our own attempts to prepare artificial hydrogenases. This can be achieved via the standard bioinspired approach using the combination of a synthetic bioinspired catalyst and a polypeptide scaffold. Such hybrid complexes provide the opportunity to optimize the system by manipulating both the catalyst through chemical synthesis and the protein component through mutagenesis. We also raise the possibility to reach such artificial systems via an original strategy based on mimicking the enzyme maturation pathways. This is illustrated in this Account by two examples developed in our laboratory. First, we show how the preparation of a lysozyme-{Mn-I(CO)(3)} hybrid and its clean reaction with a nickel complex led us to generate a new class of binuclear Ni-Mn H-2-evolving catalysts mimicking the active site of [NiFe]-hydrogenases. Then we describe how we were able to rationally design and prepare a hybrid system, displaying remarkable structural similarities to an [FeFe]-hydrogenase, and we show here for the first time that it is catalytically active for proton reduction. This system is based on the combination of HydF, a protein involved in the maturation of [FeFe]-hydrogenase (HydA), and a close mimic of the active site of this class of enzymes. Moreover, the synthetic [Fe-2(adt)(CO)(4)(CN)(2)](2-) (adt(2-) = aza-propanedithiol) mimic, alone or within a HydF hybrid system, was shown to be able to maturate and activate a form of HydA itself lacking its diiron active site. We discuss the exciting perspectives this "synthetic maturation" opens regarding the "invention" of novel hydrogenases by the chemists.

National Category
Chemical Sciences
Identifiers
urn:nbn:se:uu:diva-264087 (URN)10.1021/acs.accounts.5b00157 (DOI)000359892700022 ()26165393 (PubMedID)
Funder
Swedish Research Council Formas, 213-2014-880Swedish Research Council, 621-2014-5670Magnus Bergvall Foundation
Available from: 2015-10-05 Created: 2015-10-05 Last updated: 2017-12-01Bibliographically approved
Lundin, D., Berggren, G., Logan, D. & Sjöberg, B.-M. (2015). The Origin and Evolution of Ribonucleotide Reduction. Life, 5(1), 604-636
Open this publication in new window or tab >>The Origin and Evolution of Ribonucleotide Reduction
2015 (English)In: Life, Vol. 5, no 1, p. 604-636Article in journal (Refereed) Published
National Category
Natural Sciences
Identifiers
urn:nbn:se:uu:diva-251762 (URN)
Available from: 2015-04-24 Created: 2015-04-24 Last updated: 2015-04-24
Berggren, G., Garcia-Serres, R., Brazzolotto, X., Clemancey, M., Gambarelli, S., Atta, M., . . . Fontecave, M. (2014). An EPR/HYSCORE, Mossbauer, and resonance Raman study of the hydrogenase maturation enzyme HydF: a model for N-coordination to 4Fe-4S clusters. Journal of Biological Inorganic Chemistry, 19(1), 75-84
Open this publication in new window or tab >>An EPR/HYSCORE, Mossbauer, and resonance Raman study of the hydrogenase maturation enzyme HydF: a model for N-coordination to 4Fe-4S clusters
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2014 (English)In: Journal of Biological Inorganic Chemistry, Vol. 19, no 1, p. 75-84Article in journal (Refereed) Published
National Category
Natural Sciences
Identifiers
urn:nbn:se:uu:diva-251764 (URN)0949-8257; 1432-1327 (ISBN)
Note

Times Cited: 0

Available from: 2015-04-24 Created: 2015-04-24 Last updated: 2015-05-05
Bacchi, M., Berggren, G., Niklas, J., Veinberg, E., Mara, M. W., Shelby, M. L., . . . Artero, V. (2014). Cobaloxime-Based Artificial Hydrogenases. Inorganic Chemistry, 53(15), 8071-8082
Open this publication in new window or tab >>Cobaloxime-Based Artificial Hydrogenases
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2014 (English)In: Inorganic Chemistry, ISSN 0020-1669, E-ISSN 1520-510X, Vol. 53, no 15, p. 8071-8082Article in journal (Refereed) Published
Abstract [en]

Cobaloximes are popular H2 evolution molecular catalysts but have so far mainly been studied in nonaqueous conditions. We show here that they are also valuable for the design of artificial hydrogenases for application in neutral aqueous solutions and report on the preparation of two well-defined biohybrid species via the binding of two cobaloxime moieties, {Co(dmgH)2} and {Co(dmgBF2)2} (dmgH2 = dimethylglyoxime), to apo Sperm-whale myoglobin (SwMb). All spectroscopic data confirm that the cobaloxime moieties are inserted within the binding pocket of the SwMb protein and are coordinated to a histidine residue in the axial position of the cobalt complex, resulting in thermodynamically stable complexes. Quantum chemical/molecular mechanical docking calculations indicated a coordination preference for His93 over the other histidine residue (His64) present in the vicinity. Interestingly, the redox activity of the cobalt centers is retained in both biohybrids, which provides them with the catalytic activity for H2 evolution in near-neutral aqueous conditions.

Place, publisher, year, edition, pages
American Chemical Society, 2014
National Category
Natural Sciences
Identifiers
urn:nbn:se:uu:diva-251766 (URN)10.1021/ic501014c (DOI)
Available from: 2015-04-24 Created: 2015-04-24 Last updated: 2017-12-04
Simmons, T. R., Berggren, G., Bacchi, M., Fontecave, M. & Artero, V. (2014). Mimicking hydrogenases: From biomimetics to artificial enzymes. Coordination chemistry reviews, 270–271(0), 127-150
Open this publication in new window or tab >>Mimicking hydrogenases: From biomimetics to artificial enzymes
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2014 (English)In: Coordination chemistry reviews, ISSN 0010-8545, E-ISSN 1873-3840, Vol. 270–271, no 0, p. 127-150Article in journal (Refereed) Published
Abstract [en]

Over the last 15 years, a plethora of research has provided major insights into the structure and function of hydrogenase enzymes. This has led to the important development of chemical models that mimic the inorganic enzymatic co-factors, which in turn has further contributed to the understanding of the specific molecular features of these natural systems that facilitate such large and robust enzyme activities. More recently, efforts have been made to generate guest–host models and artificial hydrogenases, through the incorporation of transition metal-catalysts (guests) into various hosts. This adds a new layer of complexity to hydrogenase-like catalytic systems that allows for better tuning of their activity through manipulation of both the first (the guest) and the second (the host) coordination spheres. Herein we review the aforementioned advances achieved during the last 15 years, in the field of inorganic biomimetic hydrogenase chemistry. After a brief presentation of the enzymes themselves, as well as the early bioinspired catalysts, we review the more recent systems constructed as models for the hydrogenase enzymes, with a specific focus on the various strategies employed for incorporating of synthetic models into supramolecular frameworks and polypeptidic/protein scaffolds, and critically discuss the advantages of such an elaborate approach, with regard to the catalytic performances.

Keywords
Hydrogen, Hydrogenase, Biomimetic chemistry, Bioinspired chemistry, Artificial enzyme, Biohybrids, Photocatalysis, Electrocatalysis
National Category
Natural Sciences
Identifiers
urn:nbn:se:uu:diva-251763 (URN)
Available from: 2015-04-24 Created: 2015-04-24 Last updated: 2017-12-04
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-6717-6612

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