Senger M., Laun K., Soboh B. and Stripp S.T. (2018) Infrared Characterization of the Periplasmatic O2-sensitive [NiFe]-hydrogenase from E. coli. Catalysts 8(11) DOI: 10.3390/catal811053

Joern Krausze, Thomas W. Hercher, Dagmar Zwerschke, Martin L. Kirk, Wulf Blankenfeldt,Ralf R. Mendel and Tobias Kruse (2018). The functional principle of eukaryotic molybdenum insertases. Biochemical Journal, 475 1739–1753

Burschel, S., Kreuzer Decovic, D., Nuber, F., Stiller, M., Hofmann, M., Zupok, A., Siemiatkowska, B., Gorka, M., Leimkühler, S. and Friedrich,T. (2018) Iron-Sulfur Cluster Carrier Proteins Involved in the Assembly of Escherichia coliNADH:ubiquinone oxidoreductase (complex I). Mol. Microbiol., in press, (DOI) – 10.1111/mmi.14137

Freibert, S.A., Weiler, B.D., Bill, E., Pierik, A.J., Mühlenhoff, U., & Lill, R. (2018). Biochemical Reconstitution and Spectroscopic Analysis of Iron–Sulfur Proteins. Methods Enzymol. 599, 197-226.

Stehling, R., Paul, V.D., Bergmann, J., Basu, S., & Lill, R. (2018). Biochemical Analyses of Human Iron–Sulfur Protein Biogenesis and of Related Diseases. Methods Enzymol. 599, 227-263.

Torraco, A.*, Stehling, O.*, Stümpfig, C., Rösser, R., De Rasmo, D., Fiermonte, G., Verrigni, D., Rizza, T., Vozza, A., Di Nottia, M., Diodato, D., Martinelli, D., Piemonte, F., Dionisi-Vici, C., Bertini, E.#, Lill, R.# & Carrozzo, R.# (2018). ISCA1 mutation in a patient with infantile-onset leukodystrophy causes defects in mitochondrial [4Fe-4S] proteins. Hum. Mol. Genet. 27, 2739–2754. * Joint first authors; # joint corresponding authors.

Gurgel-Giannetti, J., Lynch, D.S., Brandão de Paiva, A.R., Lucato, L.T., Yamamoto, G., Thomsen, C., Basu, S., Freua, F., Giannetti, A.V., Della Ripa de Assis, B., Ribeiro, M.D.O., Barcelos, I., Souza, K.S., Monti, F., Melo, U.S., Amorim, S., Silva. L., Macedo-Souza, L.I., Vianna-Morgante, A.M., Hirano, M., Van der Knaap, M.S., Lill, R., Vainzof, M., Oldfors, A., Houlden, H., & Kok, F. (2018). A novel complex neurological phenotype due to a homozygous mutation in FDX2. Brain 141, 2289-2298. 

Ben-Shimon, L.*, Paul, V.D.*, David-Kadoch, G.*, Volpe, M., Stümpfig, M., Bill, E., Mühlenhoff, U., Lill, R.#, Ben-Aroya, S.# (2018). Fe-S cluster coordination of the chromokinesin KIF4A alters its sub-cellular localization during mitosis. J. Cell Sci. 131, jcs211433. * Joint first authors; # joint corresponding authors. Research Highlight.

Uzarska, M.A.*, Przybyla-Toscano⁠, J.*, Spantgar, F., Zannini, F., Lill, R., Mühlenhoff, U.#, & Rouhier, N.# (2018).⁠Conserved functions of Arabidopsis mitochondrial late-acting maturation factors in the trafficking of iron‑sulfur clusters. Biochim. Biophys. Acta 1865, 1250-1259. * Joint first authors; # joint corresponding authors.

Stehling, O., Jeoung, J.H., Freibert, S.A., Paul, V.D., Bänfer, S., Niggemeyer, B., Rösser, R., Dobbek, H., & Lill, R. (2018). Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins. Proc. Natl. Acad. Sci. U.S.A. 115, E9085-E9094.

Tonini, M.L., Peña-Diaz, P., Haindrich, A.C., Basu, S., Kriegová, E., Pierik, A.J., Lill, R., MacNeill, S.A., Smith, T.K., & Lukeš, J. (2018). Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei. PLOS Pathog. 14, e1007326.

Hongliang Zhang and Ute Krämer (2018) Differential Diel Translation of Transcripts With Roles in the Transfer and Utilization of Iron-Sulfur Clusters in Arabidopsis. Frontiers in Plant Science (in press) doi: 10.3389/fpls.2018.01641. accepted for publication.

Rohde, M., Trncik, C., Sippel, D., Gerhardt, S. & Einsle, O. (2018) Crystal structure of VnfH, the iron protein component of vanadium nitrogenase. J. Biol. Inorg. Chem., 23, 1049-1056.

Rohde, M., Sippel, D., Trncik, C., Andrade, S.L.A. & Einsle, O. (2018) The critical E4 state of nitrogenase catalysis. Biochemistry, 57, 5497-5504.

Sippel, D., Rohde, M., Netzer, J., Trncik, C., Gies, J., Grunau, K., Djurdjevic, I., Decamps, L., Andrade, S.L.A. & Einsle, O.(2018) A bound reaction intermediate sheds light on the mechanism of nitrogenase. Science, 359, 1484-1489.

Einsle, O. (2018) Another twist on nitrogenases. Nature Microbiol., 3, 263-264.

Sippel, D. & Einsle, O. (2017) The structure of vanadium nitrogenase reveals an unusual bridging ligand. Nature Chem. Biol., 13, 956-960.

Djurdjevic, I., Einsle, O. & Decamps, L. (2017) Nitrogenase cofactor: Inspiration for model chemistry. Chem. As. J., 12, 1447-1455.

Rees, J.A., Björnsson, R., Kowalska, J.K., Lima, F.A., Schlesier, J., Sippel, D., Weyhermüller, T., Einsle, O., Kovacs, J.A. & DeBeer, S. (2017) Comparative electronic structures of nitrogenase FeMoco and FeVco. Dalton Trans., 46, 2445-2455.

Sippel, D., Schlesier, J., Rohde, M., Trncik, C., Decamps, L., Djurdjevic, I., Spatzal, T., Andrade, S.L.A. & Einsle, O. (2017) Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion. J. Biol. Inorg. Chem., 22, 161-168.

Lena Schleicher, Valentin Muras, Björn Claußen, Jens Pfannstiel, Bastian Blombach, Pavel Dibrov, Günter Fritz, Julia Steuber (2018) Vibrio natriegens as Host for Expression of Multisubunit Membrane Protein Complexes. Front. Microbiol., 25 October 2018

Wagner, T., Huang. G., Ermler, U., Shima, S. (2018) How [Fe]-hydrogenase from Methanothermobacter is protected against light and oxidative stress. Angew. Chem. Int. Ed. 57, 15056-15059. 

Hawer H, Ütkür K, Arend M, Mayer K, Adrian L, Brinkmann U, Schaffrath R. (2018) Importance of diphthamide modified EF2 for translational accuracy and competitive cell growth in yeast. PLoS One. 13(10):e0205870.

Van Kuiken BE, Hahn AW, Nayyar B, Schiewer CE, Lee SC, Meyer F, Weyhermüller T, Nicolaou A, Cui YT, Miyawaki J, Harada Y, DeBeer S. (2018) Electronic Spectra of Iron-Sulfur Complexes Measured by 2p3d RIXS Spectroscopy. Inorg Chem. 57:7355-7361.

Mayr SJ, Sass JO, Vry J, Kirschner J, Mader I, Hövener JB, Reiss J, Santamaria-Araujo JA, Schwarz G, Grünert SC (2018) A mild case of molybdenum cofactor deficiency defines an alternative route of MOCS1 protein maturation. J Inherit Metab Dis.. doi: 10.1007/s10545-018-0138-7.

Huang, G., Wagner, T., Ermler, U. Bill, E., Ataka, K. and Shima, S. (2018) O2 sensitivity of [Fe]-hydrogenase in the presence of reducing substrates. Angew Chem Int Ed in press. DOI: 10.1002/anie.201712293 and 10.1002/ange.201712293.

Wagner, T., Ermler, U. & Shima, S. (2018) Tungsten-containing formylmethanofuran dehydrogenase. In Encyclopedia of Inorganic and Bioinorganic Chemistry (online). (A. Messerschmidt, Albrecht ed.) John Wiley and Sons, Inc..

Wagner, T., Watanabe, T. & Shima, S. (2018) Hydrogenotrophic methanogenesis. In Handbook of Hydrocarbon and Lipid Microbiology Series. Biogenesis of Hydrocarbons (A.J.M. Stams and D.Z. Sousa eds.) Springer, Germany.


>> 2017

Schmitt G., Arndt F., Kahnt J., Heider J. (2017) Adaptations to a loss-of-function mutation in the betaproteobacterium Aromatoleum aromaticum: recruitment of alternative enzymes for anaerobic phenylalanine degradation. J. Bacteriol. 199, e00383-17. doi: 10.1128/JB.00383-17.

Kaufholdt D, Baillie CK, Meinen R, Mendel RR, Hänsch R (2017). The Molybdenum Cofactor Biosynthesis Network: In vivo Protein-Protein Interactions of an Actin Associated Multi-Protein Complex. Frontiers in Plant Science, 8, 1946.
Krausze J, Probst C, Curth U, Reichelt J, Saha S, Schafflick D, Heinz DW,  Mendel RR, Kruse T (2017). Synthesis of the Molybdenum Cofactor: Dimerization of the plant enzyme Cnx1E is required for substrate binding. Biochemical Journal, 474, 163–178. 

Braymer, J.J. & Lill, R. (2017). Iron-sulfur cluster biogenesis and trafficking in mitochondria. J. Biol. Chem. 292, 12754–12763.

208) Boniecki, M.T.*, Freibert, S.A.*, Mühlenhoff, U., Lill, R.#, & Cygler, M.# (2017). Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex. Nat. Commun. 8, 1287. * Joint first authors; # joint corresponding authors.

Sokołowski M, Klassen R, Bruch A, Schaffrath R, Glatt S (2017) Cooperativity between different tRNA modifications and their modification pathways. Biochim Biophys Acta [Epub ahead of print] doi: 10.1016/j.bbagrm.2017.12.003

Wagner, T., Koch, J., Ermler, U. & Shima, S. (2017) Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction. Science 357, 699–703.

Bai, L., Wagner, T., Xu, T., Hu, X., Ermler, U. & Shima, S. (2017) Water-bridged H-bonding network contributes to the catalysis of a SAM-dependent C-methyltransferase HcgC. Angew Chem Int Ed 56, 10806–0809.

Bai, L., Fujishiro, T., Huang, G., Koch, J., Takabayashi, A., Yokono, M., Tanaka, A., Xu, T., Hu, X., Ermler, U. & Shima, S. (2017) Towards artificial methanogenesis: biosynthesis of the [Fe]-hydrogenase cofactor and characterization of the semisynthetic hydrogenase. Faraday Discussion, 2017, 198, 37-58.

Senger, M., Stripp, S.T., Soboh, B. (2017) Proteolytic Cleavage Orchestrates Cofactor Insertion and Protein Assembly in [NiFe]-hydrogenase Biosynthesis. J Biol Chem. (28):11670-11681. 

Adamson H, Robinson M, Bond PS, Soboh B, Gillow K, Simonov AN, Elton DM, Bond AM, Sawers RG, Gavaghan DJ, Parkin A. (2017) Analysis of HypD Disulfide Redox Chemistry via Optimization of Fourier Transformed ac Voltammetric Data. Anal Chem. (3):1565-1573.

Dörner K, Vranas M, Schimpf J, Straub IR, Hoeser J and Friedrich T (2017) Significance of the [2Fe-2S] Cluster N1a for Electron Transfer and Assembly of Escherichia coli Respiratory Complex I. Biochemistry, 56, 2770-2778. DOI: 10.1021/acs.biochem.6b01058

S. Müller, H. Auerbach, K. Stegmaier, J. A. Wolny, V. Schünemann, A. J. Pierik (2017) Mössbauer spectroscopy and DFT calculations on all protonation states of the 2Fe-2S cluster of the Rieske protein. Hyperfine Interact (2017) 238: 102

Schmitt G, Arndt F, Kahnt J, Heider J. (2017) Adaptations to a Loss-of-Function Mutation in the Betaproteobacterium Aromatoleum aromaticum: Recruitment of Alternative Enzymes for Anaerobic Phenylalanine Degradation. J Bacteriol. 199: e00383-17.

Schaffrath R, Leidel SA (2017) Wobble uridine modifications – a reason to live, a reason to die?! RNA Biol 14, 1209-1222.

Berndt, C., and Lillig, C.H. (2017) Glutathione, Glutaredoxins, and iron. Antioxid. Redox Signal. 27: 1235-1251 

Lepka, K., Volbracht, K., Bill, E., Schneider, R., Rios, N., Hildebrandt, T., Ingwersen, J., Prozorovski, T., Lillig, C.H., van Horssen, J., Steinman, L., Hartung, H.-P., Radi, R., Holmgren, A., Aktas, O., and Berndt, C. (2017) Iron-sulfur Glutaredoxin 2 protects oligodendrocytes against damage induced by nitric oxide released from activated microglia. Glia 65: 1521-1534

Moore SJ, Sowa ST, Schuchardt C, Deery E, Lawrence AD, Ramos JV, Billig S, Birkemeyer C, Chivers PT, Howard MJ, Rigby SE, Layer G, Warren MJ (2017) Elucidation of the biosynthesis of the methane catalyst coenzyme F430. Nature 543:78-82.

Bühning M, Friemel M, Leimkühler S (2017) Functional Complementation Studies Reveal Different Interaction Partners of Escherichia coli IscS and Human NFS1. Biochemistry 56:4592-4605

Bühning M, Valleriani A, Leimkühler S (2017) The Role of SufS Is Restricted to Fe-S Cluster Biosynthesis in Escherichia coli. Biochemistry 56:1987-2000.

Leimkühler S (2017) Shared function and moonlighting proteins in molybdenum cofactor biosynthesis. Biol Chem 398:1009-1026.

Lindenstrauß U, Skorupa P, McDowall JS, Sargent F and C Pinske (2017) The dual-function chaperone HycH improves assembly of the formate hydrogenlyase complex.  Biochem J 2017, BCJ20170431

J. K. Kowalska, B. Nayyar, J. A. Rees, C. E. Schiewer, S. C. Lee, J. A. Kovacs, F. Meyer, T. Weyhermuller, E. Otero and S. DeBeer (2017) Iron L2,3-Edge X‑ray Absorption and X-ray Magnetic Circular Dichroism Studies of Molecular Iron Complexes with Relevance to the FeMoco and FeVco Active Sites of Nitrogenase Inorg. Chem. 2017, 56, 8147−8158, DOI:10.1021/acs.inorgchem.7b00852.

Bergner M., L. Roy, S. Dechert, F. Neese, Shengfa Ye, and F. Meyer (2017) Ligand Rearrangements at Fe/S Cofactors: Slow Isomerization of a Biomimetic [2Fe-2S] Cluster Angew. Chem. Int. Ed. 2017, 56, 4882–4886

Marie Bergner, Sebastian Dechert, Serhiy Demeshko, Claudia Kupper, James M. Mayer, and Franc Meyer 
 (2017) Model of the MitoNEET [2Fe−2S] Cluster Shows Proton Coupled Electron Transfer J. Am. Chem. Soc., 139: 701-707.

Sippel, D., Schlesier, J., Rohde, M., Trncik, C., Decamps, L., Djurdjevic, I., Spatzal, T., Andrade, S.L.A. & Einsle, O. (2017) Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion. J. Biol. Inorg. Chem., in press.


>> 2016

Schmid, G., Auerbach, H., Pierik, A.J., Schünemann, V. & Boll, M. (2016)  ATP-dependent electron activation module of benzoyl-coenzyme A reductase from the hyperthermophilic archaeon Ferroglobus placidus. Biochemistry 55, 5578-5586.

Uzarska, M.A.*, Nasta, V.*, Weiler, B.D.*, Spantgar, F., Ciofi-Baffoni, S., Saviello, M.R., Gonnelli, L., Mühlenhoff, U., Banci, L.#, & Lill, R.# (2016). Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins. eLife 5, e16673. * Joint first authors; # joint corresponding authors.

Melber, A,. Na, U., Vashisht, A., Weiler, B.D., Lill, R., Wohlschlegel, J.A., & Winge, D.R. (2016). Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients. eLife 5, e15991.

Jüdes A, Bruch A, Klassen R, Helm M, Schaffrath R (2016) Sulfur transfer and activation by ubiquitin-like modifier system Uba4•Urm1 link protein urmylation and tRNA thiolation in yeast. Microb Cell 3, 554-564.

Bürstel, I. , E. Siebert , S. Frielingsdorf , I. Zebger , B. Friedrich & O. Lenz (2016) 

Synthesis of CO from the central one-carbon pool: origin of the carbonyl ligand in O2-tolerant [NiFe]-hydrogenase. 
Proc. Natl. Acad. Sci. U. S. A. 113:14722-14726.

Iñigo S, Nagels Durand A, Ritter A, Le Gall S, Termathe M, Klassen R, Tohge T, De Coninck B, De Clercq R, Cammue B, Fernie AR, Gevaert K, De Jaeger G, Leidel S, Schaffrath R, Van Lijsebettens M, Pauwels L, Goossens A (2016) Glutaredoxin GRXS17 associates with the Arabidopsis cytosolic iron-sulfur cluster assembly pathway. Plant Physiol 172, 858-873.