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2023

  • Trncik, C., Detemple, F. & Einsle, O. (2023) Iron-based Biological Nitrogen Fixation: Fe-Nitrogenase underscores common principles of Nitrogenase Catalysis. Nat. Catal., 6, 415-424.
  • Lycus, P., Einsle, O. & Zhang, L. (2023) Structural Biology of Proteins involved in nitrogen cycling. Curr. Op. Chem. Biol., 74, 102278.
  • Martin Del Campo, J.S., Rigsbee, J., Bueno Batista, M., Mus, F., Rubio, L.M., Einsle, O., Peters, J.W., Dixon, R., Dean, D.R., & Dos Santos, P.C. (2023) Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in Azotobacter vinelandii. Crit. Rev. Biochem. Mol. Biol., 6, 1-47.
  • Warstat, R., Pervaiz, M., Regenass, P., Amann, M., Schmidtkunz, K., Einsle, O., Jung, M., Breit, B., Hügle, M., & Günther, S. (2023) A novel pan-selective bromodomain inhibitor for epigenetic drug design. Eur. J. Med. Chem., 248, 115139.
  • Stephens, I.E.L., Chan, K., Bagger, A., Boettcher, S.W., Bonin, J., Boutin, E., Buckley, A., Buonsanti, R., Cave, E., Chang, X., Chee, S.W., da Silva, A.H.M., de Luna, P., Einsle, O., Endrödi, B., Escudero-Escribano, M., Ferreira de Araujo, J.V., Figueiredo, M.C., Hahn, C., Hansen, K.U., Haussener, S., Hunegnaw, S., Huo, Z., Hwang, Y.J., Janáky, C., Jayathilake, B.S., Jiao, F., Jovanov, Z.P., Karimi, P., Koper, M.T.M., Kuhl, K., Lee, W.H., Liang, Z., Liu, X., Ma, S., Ma, M., Oh, H.S., Robert, M., Roldan Cuenya, B., Rossmeisl, J., Roy, C., Ryan, M.P., Sargent, E.H., Sebastián-Pascual, P., Seger, B., Steier, L., Strasser, P., Varela, A.S., Vos, R.E., Wang, X., Xu, B., Yadegari, H. & Zhou, Y. (2023) 2022 roadmap on low temperature electrochemical CO reduction. J. Phys. Energy, in press.
  • Su, C., Rodriguez-Franco, M., Lace, B., Nebel, N., Hernandez-Reyes, C., Liang, P., Schulze, E., Mymrikov, E.V., Gross, N.M., Knerr, J., Wang, H., Siukstaite, L., Keller, J., Libourel, C., Fischer, A.A.M., Gabor, K.E., Mark, E., Popp, C., Hunte, C., Weber, W., Wendler, P., Stanislas, T., Delaux, P.M., Einsle, O., Grosse, R., Römer, W., & Ott, T. (2023) Stabilization of membrane topologies by proteinaceous remorin scaffolds. Nat. Commun., 14, 323-328.
  • Zhang, L. & Einsle, O. (2022) Architecture of the NADH:ferredoxin oxidoreductase RNF that drives biological nitrogen fixation. biorXiv.

 

2022

  • Müller, C., Zhang, L., Zipfel, S., Topitsch, A., Lutz, M., Eckert, J., Prasser, B., Chami, M., Lü, W., Du, J. & Einsle, O. (2022) Molecular interplay of an assembly machinery for nitrous oxide reductase. Nature, 606, 626-632.
  • Hoeser, F., Tausend, H., Götz, S., Wohlwend, D., Einsle, O., Günther, S. & Friedrich, T. (2022) Respiratory complex I with charge symmetry in the membrane arm pumps protons. Proc. Natl. Acad. Sci. USA, 119, e2123090119.
  • Vogelmann, A., Schiedel, M., Wössner, N., Merz, A., Herp, D., Hammelmann, S., Colcerasa, A., Komaniecki, G., Hong, J.Y., Sum, M., Metzger, E., Neuwirt, E., Zhang, L., Einsle, O., Groß, O., Schüle, R., Lin, H., Sippl, W. & Jung, M. (2022) Development of a NanoBRET assay to validate inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration. RSC Chem. Biol., 3, 468-485.

 

2021

  • Trncik, C., Müller, T., Franke, P. & Einsle, O. (2021) Structural analysis of the reductase component AnfH of iron-only nitrogenase from Azotobacter vinelandii. J. Inorg. Biochem, 277, 111690.
  • Vranas, M., Wohlwend, D., Qiu, D., Gerhardt, S., Trncik, C., Pervaiz, M., Ritter, K., Steimle, S., Randazzo, A., Einsle, O., Günther, S., Jessen, H.J., Kotlyar, A. & Friedrich, T. (2021) Structural Basis for Inhibition of ROS-Producing Respiratory Complex I by NADH-OH. Angew. Chem. Intl. Ed., 60, 27277-27281.
  • Sartor, P., Denkhaus, L., Gerhardt, S., Einsle, O. & Fetzner, S. (2021) Structural basis of O-methylation of (2-heptyl-)1-hydroxyquinolin-4(1H)-one and related compounds by the heterocyclic toxin methyltransferase Rv0560c of Mycobacterium tuberculosis. J. Struct. Biol., 213, 107794.
  • Parison, K., Gies-Elterlein, J., Trncik, C. & Einsle, O. (2021) Expression, isolation, and characterization of vanadium nitrogenase from Azotobacter vinelandii. Methods Mol. Biol., 2353, 97-121.
  • Pérez-González, A., Jimenez-Vicente, E., Gies-Elterlein, J., Salinero-Lanzarote, A., Yang, Z.Y., Einsle, O., Seefeldt, L. & Dean, D.R. (2021) Specificity of NifEN and VnfEN for the assembly of nitrogenase active site cofactors in Azotobacter vinelandii. mBio, 12, e0156821.
  • Prasser, B., Schöner, L., Zhang, L. & Einsle, O. (2021) The copper chaperone NosL forms a heterometal site for Cu delivery to nitrous oxide reductase. Angew. Chem. Intl. Ed., 60, 18810-18814.
  • Rohde, M., Laun, K., Zebger, I., Stripp, S.T. & Einsle, O. (2021) Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle. Sci. Adv., 7, eabg4474.
  • Schultenkämper, K., Gütle, D.D., López, M.G., Keller, L.B., Zhang, L., Einsle, O., Jacquot, J.P. & Wendisch, V.F. (2021) Interrogating the Role of the Two Distinct Fructose-Bisphosphate Aldolases of Bacillus methanolicus by Site-Directed Mutagenesis of Key Amino Acids and Gene Repression by CRISPR Interference. Front. Microbiol., 12, 669220.
  • Brausemann, A., Zhang, L., Ilcu, L. & Einsle, O. (2021) Architecture of the membrane-bound cytochrome c heme lyase CcmF. Nat. Chem. Biol., 17, 800-805.
  • Alali, A., Zhang, L., Li, J., Zuo, C., Wassouf, D., Yan, X., Schwarzer, P., Günther, S., Einsle, O. & Bechthold, A. (2021) Biosynthesis of the Tricyclic Aromatic Type II Polyketide Rishirilide: New Potential Third Ring Oxygenation after Three Cyclization Steps. Mol. Biotechnol., 63, 502-514.
  • Peters, J.W., Einsle, O., Dean, D.R., DeBeer, S., Hoffman, B.M., Holland, P.L. & Seefeldt, L.C. (2021) Comment on "Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase". Science, 371, eabe5481.
  • Zhang, L., Bill, E., Kroneck, P.M.H. & Einsle, O. (2021) A [3Cu:2S] cluster provides insight into the assembly and function of the CuZ site of nitrous oxide reductase. Chem. Sci., 12, 3239-3244.
  • Zhang, L., Bill, E., Kroneck, P.M.H. & Einsle, O. (2021) Histidine-Gated Proton-Coupled Electron Transfer to the CuA Site of Nitrous Oxide Reductase. J. Am. Chem. Soc., 143, 830-838.

 

2020

  • Hügle, M., Regenass, P., Warstat, R., Hau, M., Schmidtkunz, K., Lucas, X., Wohlwend, D., Einsle, O., Jung, M., Breit, B. & Günther, S. (2020) 4-Acyl Pyrroles as Dual BET-BRD7/9 Bromodomain Inhibitors Address BETi Insensitive Human Cancer Cell Lines. J. Med. Chem., 63, 15603-15620.
  • Jagilinki, B.P., Ilic, S., Trncik, C., Tyryshkin, A.M., Pike, D.H., Lubitz, W., Bill, E., Einsle, O., Birrell, J.A., Akabayov, B., Noy, D. & Nanda, V. (2020) In Vivo Biogenesis of a De Novo Designed Iron-Sulfur Protein. ACS Synth. Biol., 9, 3400-3407.
  • Rohde, M., Grunau, K. & Einsle, O. (2020) CO binding to the FeV Cofactor of CO-reducing Vanadium Nitrogenase at Atomic Resolution. Angew. Chem. Intl. Ed., 59, 23626-23630.
  • Djurdjevic, I., Trncik, C., Rohde, M., Gies-Elterlein, J., Grunau, K., Schneider, F., Andrade, S.L. & Einsle, O. (2020) The Cofactors of Nitrogenases. Met. Ions Life Sci., 20, 257-312.
  • Schiedel, M., Lehotzky, A., Szunyogh, S., Oláh, J., Hammelmann, S., Wössner, N., Robaa, D., Einsle, O., Sippl, W., Ovádi, J. & Jung, M. (2020) HaloTag-Targeted Sirtuin-Rearranging Ligand (SirReal) for the Development of Proteolysis-Targeting Chimeras (PROTACs) against the Lysine Deacetylase Sirtuin 2 (Sirt2). ChemBioChem, 21, 3371-3376.
  • Einsle, O. & Rees, D.C. (2020) Structural Enzymology of Nitrogenase Enzymes. Chem. Rev. 120, 4969-5004.
  • Wössner, N., Alhalabi, Z., González, J., Swyter, S., Gan, J., Schmidtkunz, K., Zhang, L., Vaquero, A., Ovaa, H., Einsle, O., Sippl, W. & Jung, M. (2020) Sirtuin 1 Inhibiting Thiocyanates (S1th)-A New Class of isotype Selective Inhibitors of NAD+ Dependent Lysine Deacetylases. Front. Oncol., 10, 657.
  • Grathwol, C.W., Wössner, N., Behnisch-Cornwell, S., Schulig, L., Zhang, L., Einsle, O., Jung, M. & Link, A. (2020) Activation of Sirtuim 2 Inhibitors Employing Photoswitchable Geometry and Aqueous Solubility. ChemMedChem, 15, 1480-1489.
  • Jasper, J., Ramos, J.V., Trncik, C., Jahn, D., Einsle, O., Layer, G., Moser, J. (2020) Chimeric Interaction of Nitrogenase-Like Reductases with the MoFe Protein of Nitrogenase. ChemBioChem, 21, 1733-1741.

 

2019

  • Hickey, D.P., Cai, R., Yang, Z.Y., Grunau, K. Einsle, O., Seefeldt, L.C. & Minteer, S.D. (2019) Establishing a Thermodynamic Landscape for the Active Site of Mo-Dependent Nitrogenase. J. Am. Chem. Soc., 30, 17150-17157.
  • Rohde, M., Grunau, K., Djurdjevic, I., Trncik, C., Schneider, F., Gies-Elterlein, J. & Einsle, O.(2019) Vanadium nitrogenase. In: Encyclopedia of Inorganic and Bioinorganic Chemistry, Messerschmidt, A. (ed). DOI: 10.1002/9781119951438.eibc2698.
  • Costa, N.L., Hermann, B., Fourmond, V., Faustino, M.M., Teixeira, M., Einsle, O., Paquete, C.M. & Louro, R.O. (2019) How Thermophilic Gram-Positive Organisms Perform Extracellular Electron Transfer: Characterization of the Cell Surface Terminal Reductase OcwA. mBio, 10, e01210-e01219.
  • Harris, D.F., Lukoyanov, D.A., Kallas, H., Trncik, C., Yang, Z.Y., Compton, P., Kelleher, N., Einsle, O., Dean, D.R., Hoffman, B.M. & Seefeldt, L.C. (2019) Mo-, V-, and Fe-Nitrogenases Use a Universal Eight-Electron Reductive-Elimination Mechanism To Achieve N2 Reduction. Biochemistry, 58, 3293-3301.
  • Zhang, L., Wüst, A., Prasser, B., Müller, C. & Einsle, O. (2019) Functional assembly of nitrous oxide reductase provedes insights into copper site maturation. Proc. Natl. Acad. Sci. USA, 116, 12822-12827.
  • Schulte, M., Frick, K., Gnandt, E., Jurkovic, S., Burschel, S., Labatzke, R., Aierstock, K., Fiegen, D., Wohlwend, D., Gerhardt, S., Einsle, O. & Friedrich, T. (2019) A mechanism to prevent production of reactive oxygen species by Escherichia coli complex I. Nature Comm., 10, 2551.
  • Kowalska, J.K., Henthorn, J.T., Van Stappen, C., Trncik, C., Einsle, O., Keavney, D. & DeBeer, S. (2019) X-ray magnetic circular dichroism spectroscopy applied to nitrogenase and related models: Experimental Evidence for a spin-coupled Molybdenum(III) center. Angew. Chem. Intl. Ed., 58, 9373-9377.
  • Metzger, E., Wang, S., Urban, S., Willmann, D., Schmidt, A., Offermann, A., Allen, A., Sum, M., Obier, N., Cottard, F., Ulferts, S., Preca, B.T., Hermann, B., Maurer, J., Greschik, H., Hornung, V., Einsle, O., Perner, S., Imhof, A., Jung, M. & Schüle, R. (2019) KMT9 monomethylates histone H4 lysine 12 and controls proliferation of prostate cancer cells. Nature Struct. Mol. Biol., 26, 361-371.
  • Li, M., Müller, C., Fröhlich, K., Gorka, O., Zhang, L., Groß, O., Schilling, O., Einsle, O. & Jessen-Trefzer, C. (2019) Detection and characterization of a mycobacterial L-arabinofuranose ABC transporter identified with a rapid lipoproteomics protocol. Cell Chem. Biol., 26, 852-862.

 

2018

  • 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.
  • Parnell, A.E., Mordhorst, S., Kemper, F., Giurrandino, M., Prince, J.P., Schwarzer, N.J., Hofer, A., Wohlwend, D., Jessen, H.J., Gerhardt, S., Einsle, O., Oyston, P.C.F., Andexer, J.N. & Roach, P.L. (2018) Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures. Proc. Natl. Acad. Sci. USA, 115, 3350-3355.
  • Einsle, O. (2018) Another twist on nitrogenases. Nature Microbiol., 3, 263-264.

 

2017

  • Hügle, M., Lucas, X., Ostrovskyi, D., Regenass, P., Gerhardt, S., Einsle, O., Hau, M., Jung, M., Breit, B., Günther, S. & Wohlwend, D. (2017) Beyond the BET family: targeting CBP/p300 with 4-acyl pyrroles. Angew. Chem. Intl. Ed., 56, 12476-12480.  
  • Sippel, D. & Einsle, O. (2017) The structure of vanadium nitrogenase reveals an unusual bridging ligand. Nature Chem. Biol., 13, 956-960.
  • Brausemann, A., Gemmecker, S., Koschmieder, J., Ghisla, S., Beyer, P. & Einsle, O. (2017) Structure of phytoene desaturase provides insights into herbicide binding and reaction mechanisms involved in carotene desaturation. Structure, 25, 1222-1232.
  • Ilcu, L., Röther, W., Birke, J., Brausemann, A., Einsle, O. & Jendrossek, D. (2017) Structural and functional analysis of latex clearing protein (Lcp) provides insight into the enzymatic cleavage of rubber. Sci. Rep., 7, 6179.
  • Dantas, J.M., Brausemann, A., Einsle, O. & Salgueiro, C.A. (2017) NMR studies of the interaction between inner membrane-associated and periplasmic cytochromes from Geobacter sulfurreducens. FEBS Lett., 591, 1657-1666.
  • Djurdjevic, I., Einsle, O. & Decamps, L. (2017) Nitrogenase cofactor: Inspiration for model chemistry. Chem. As. J., 12, 1447-1455.
  • Haase, D., Hermann, B., Einsle, O. & Simon, J. (2017) Epsilonproteobacterial hydroxylamine oxidoreductase (εHao): Characterization of a 'missing link' in the multihaem cytochrome c family. Mol. Microbiol., 105, 127-138. 
  • 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.
  • Siegrist, J., Netzer, J., Mordhorst, S., Karst, L., Gerhardt, S., Einsle, O., Richter, M. & Andexer, J.N. (2017) Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity. FEBS Lett., 591, 312-321. 

 

2016

  • Conradt, D., Hermann, B., Gerhardt, S., Einsle, O. & Müller, M. (2016) Biocatalytic properties and structural analysis of phologlucinol reductases. Angew. Chem. Intl. Ed., 55, 15531-15534.
  • Zhang, L., Trncik, C., Andrade, S.L.A. & Einsle, O. (2016) The flavinyl transferase ApbE of Pseudomonas stutzeri matures the NosR protein required for nitrous oxide reduction. BBA - Bioenergetics, 1858, 95-102.
  • Gütle, D.D., Roret, T., Müller, S.J., Couturier, J., Lemaire, S.D., Hecker, A., Dhalleine, T., Buchanan, B.B., Reski, R., Einsle, O. & Jacquot, J.-P. (2016) Chloroplast FBPase and SBPase are thioredoxin-linked enzymes with similar architecture but different evolutionary histories. Proc. Natl. Acad. Sci. USA, 113, 6779-6784. 
  • Hügle, M., Lucas, X., Weitzel, G., Ostrovskyi, D., Breit, B., Gerhard, S., Schmidtkunz, K., Jung, M., Schüle, R., Einsle, O., Günther, S. & Wohlwend, D. (2016) Preparation data of the bromodomains BRD3(1), BRD3(2), BRD4(1), and BRPF1B and crystallization of BRD4(1)-inhibitor complexes. Data Brief, 7, 1370-1374. 
  • Andrade, S.L.A. & Einsle, O. (2016) Channels and Transporters for Nitrogen Cycle Intermediates, In: Metalloenzymes in Denitrification: Applications and Environmental Impacts. (Moura, I., Moura, J.J.G., Pauleta, S.R. & Maia, L., eds.), RSC Publishing, Oxford, 287-311. 
  • Boll, M., Einsle, O., Ermler, U., Kroneck, P.M.H. & Ullmann, G.M. (2016) Structure and function of the unusual tungsten enzymes acetylene hydrates and class II benzoyl-coenzyme A reductase. J. Mol. Microbiol. Biotechnol., 26, 119-137. 
  • Rabus, R., Boll, M., Heider, J., Meckenstock, R.U., Buckel, W., Einsle, O., Ermler, U., Golding, B.T., Gunsalus, R.P., Kroneck, P.M.H., Krueger, M., Lueders, T., Martins, B.M., Musat, F., Richnow, H.H., Schink, B., Seifert, J., Szaleniec, M., Treude, T., Ullmann, G.M., Vogt, C., von Bergen, M. & Wilkes, H. (2016) Anaerobic microbial degradation of hydrocarbons: From enzymatic reactions to the environment. J. Mol. Microbiol. Biotechnol., 26, 5-28.
  • Schneider, L.K. & Einsle, O. (2016) The role of calcium in secondary structure stabilization during maturation of nitrous oxide reductase. Biochemistry, 55, 1433-1440. 
  • Spatzal, T., Schlesier, J., Burger, E.-M., Sippel, D., Zhang, L., Andrade, S.L.A., Rees, D.C. & Einsle, O. (2016) Nitrogenase FeMoco investigated by spatially-resolved anomalous dispersion refinement. Nature Commun., 7, 10902.
  • Brausemann, A., Gerhardt, S., Schott, A.K., Einsle, O., Große-Berkenbusch, A., Johnson, N. & Gronemeyer, T. (2016) Crystal structure of Cdc11, a septin subunit from Saccharomyces cerevisiae. J. Struct. Biol., 193, 157-161.
  • Metzger, E., Willmann, D., McMillan, J., Forne, I., Metzger, P., Gerhardt, S., Petroll, K., von Maessenhausen, A., Urban, S., Schott, A.K., Espejo, A., Eberlin, A., Wohlwend, D., Schüle, K.M., Schleicher, M., Perner, S., Bedford, M.T., Jung, M., Dengjel, J., Flaig, R., Imhof, A., Einsle, O. & Schüle, R. (2016) Assembly of methylated LSD1 and CHD1 drives AR-dependent transcription and translocation. Nature Struct. Mol. Biol., 23, 132-139.
  • Schiedel, M., Rumpf, T., Karaman, B., Lehotzky, A., Gerhardt, S., Ovádi, J., Sippl, W., Einsle, O. & Jung, M. (2016) Structure-based development of a Sirtuin 2 affinity probe. Angew. Chem. Intl. Ed., 55, 2252-2256.
  • Hügle, M., Lucas, X., Weitzel, G., Ostrovskyi, D., Breit, B., Gerhardt, S., Einsle, O., Günther, S. & Wohlwend, D. (2016) 4-acyl pyrrole derivatives yield novel vectors for designing inhibitors of the acetyl-lysine recognition site of BRD4(1). J. Med. Chem., 59, 1518-1530.
  • Schiedel, M., Rumpf, T., Karaman, B., Lehotzky, A., Oláh, J., Gerhardt, S., Ovádi, J., Sippl, W., Einsle, O. & Jung, M. (2016) Aminothiazoles as potent and selective Sirt2-inhibitors - a structure-activity relationship study. J. Med. Chem., 59, 1599-1612.
  • Newie, J., Andreou, A., Neumann, P., Einsle, O., Feußner, I. & Ficner, R. (2016) Crystal structure of a lipoxygenase from Cyanothece sp. may reveal novel features for substrate acquisition. J. Lipid. Res., 57, 276-287.
  • Schlesier, J., Rohde, M., Gerhardt, S. & Einsle, O. (2016) A conformational switch triggers nitrogenase protection from oxygen damage by Shethna protein II (FeSII). J. Am Chem. Soc., 138, 239-247.

 

2015

  • Rumpf, T., Gerhardt, S., Einsle, O. & Jung, M. (2015) Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking. Acta Cryst., F71, 1498-1510.
  • Brausemann, A., Seidel, J., Wüst, A. & Einsle, O. (2015) Multiheme Peroxidases. In: Heme Peroxidases (Raven, E.L. & Dunford, H.B., eds.) RSC Publishing, Oxford, 113-132.
  • Rees, J.A., Björnsson, R., Schlesier, J., Sippel, D., Einsle, O. & DeBeer, S. (2015) The Fe-V cofactor of vanadium nitrogenase contains an interstitial carbon atom. Angew. Chem. Intl. Ed., 54, 13249-13252. 
  • Burger, E.-M., Andrade, S.L.A. & Einsle, O. (2015) Active sites without restraints: high-resolution analysis of metal cofactors. Curr. Op. Struct. Biol. 35, 32-40.
  • Gemmecker, S., Schaub, P., Koschmieder, J., Brausemann, A., Drepper, F., Rodriguez-Franco, M., Ghisla, S., Warscheid, B., Einsle, O. & Beyer, P. (2015) Phytoene desaturase from Oryza sativa: Oligomeric Assembly, Membrane Association and preliminary 3D analysis. PLoS ONE, 10, e0131717.
  • Cahn, J.K., Brinkmann-Chen, S., Spatzal, T., Wiig, J.A., Buller, A.R., Einsle, O., Hu, Y., Ribbe, M.W. & Arnold, F.H. (2015) Cofactor specificity and the induced fit mechanism in Class I ketol-acid reductoisomerases. Biochem. J., 468, 475-484.
  • Morrisson, C.N., Hoy, J.A., Zhang, L., Einsle, O. & Rees, D.C. (2015) Substrate pathways in the nitrogenase MoFe protein by experimental identification of small-molecule binding sites. Biochemistry, 54, 2052-2060.
  • Hermann, B., Kern, M., La Pietra, L., Simon, J. & Einsle, O. (2015) The octahaem MccA is a haem c–copper sulfite reductase. Nature, 520, 706-709.
  • Rumpf, T., Schiedel, M., Karaman, B., Roessler, C., North, B.J., Lehotzky, A., Ladwein, K.I., Schmidtkunz, K:, Gaier, M., Pannek, M., Steegborn, C., Sinclair, D.A., Gerhardt, S., Ovádi, J., Schutkowski, M., Sippl, W., Einsle, O. & Jung, M. (2015) Selective Sirt2-inhibition by ligand-induced rearrangement of the active site. Nature Commun., 6, 6263.
  • Rycovska-Blume, A., Lü, W., Andrade, S., Fendler, K. & Einsle, O. (2015) Structural and functional studies of NirC from Salmonella typhimurium. Meth. Enzymol., 556, 475-497.
  • Björnsson, R., Neese, F., Schrock, R.R., Einsle, O. & DeBeer, S. (2015) The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry. J. Biol. Inorg. Chem., 20, 447-460.
  • Tam, H.K., Härle, J., Gerhardt, S., Rohr, J., Wang, G., Thorson, J.S., Bigot, A., Lutterbeck, M., Seiche, W., Breit, B., Bechthold, A. & Einsle, O. (2015) Structural characterization of O- and C-glycosylating landomycin glycosyltransferases. Angew. Chem. Intl. Ed., 54, 2811-2815.
  • Björnsson, R., Delgado-Jaime, M.U., Lima, F.A., Sippel, D., Schlesier, J., Weyhermüller, T., Einsle, O., Neese, F. & DeBeer, S. (2015) Molybdenum L-Edge XAS Spectra of MoFe Nitrogenase. Z. Allg. Anorg. Chem., 641, 65-71.

 

2014

  • Schneider, L.K., Wüst, A., Pomowski, A., Zhang, L. & Einsle, O. (2014) No laughing matter: the unmaking of the greenhouse gas dinitrogen monoxide by nitrous oxide reductase. Met. Ions Life Sci., 14, 177-210.
  • Spatzal, T., Perez, K.A., Einsle, O., Howard, J.B. & Rees, D.C. (2014) Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase. Science, 345, 1620-1623.
  • Kükenshöner, T., Hagemann, U.B., Wohlwend, D., Räuber, C., Baumann, T., Keller, S., Einsle, O., Müller, K.M. & Arndt, K.M. (2014) Selection and design analysis of chimeric D- and L-α-helix assemblies. Biomacromolecules, 15, 3296-3305. 
  • Einsle, O. (2014) Connecting Photosynthetic Light Harvesting and Charge Separation at Higher Detail. Angew. Chem. Intl. Ed., 53, 7988-7990.
  • Huber, T., Schneider, L., Präg, A., Gerhardt, S., Einsle, O. & Müller, M. (2014) Direct reductive amination of ketones: Structure and Activity of S-Selective Imine Reductases from Streptomyces. ChemCatChem, 6, 2248-2252.
  • Frick, E., Spatzal, T., Gerhardt, S., Krämer, A., Einsle, O. & Hüttel, W. (2014) Structural and functional characterization of 4-hydroxyphenylpyruvate dioxygenase from the thermoacidophilic archaeon Picrophilus torridus. Extremophiles, 18, 641-651.
  • Björnsson, R., Lima, F.A., Spatzal, T., Weyhermüller, T., Glatzel, P., Bill, E., Einsle, O., Neese, F. & DeBeer, S. (2014) Identification of a spin-coupled Mo(III) in the Nitrogenase Iron-Molybdenum Cofactor. Chem. Sci., 5, 3096-3103. 
  • Spatzal, T., Andrade, S.L.A. & Einsle, O. (2014) The Iron-Molybdenum Cofactor of Nitrogenase. In: Iron-Sulfur Clusters in Chemistry and Biology (Rouault, T., ed.); Walter de Gruyter; pp.89-105.
  • Kükenshöner, T., Wohlwend, D., Niemöller, C., Dondapati, P., Speck, J., Adeniran, A.V., Nieth, A., Gerhardt, S., Einsle, O., Müller, K.M. & Arndt, K.M. (2014) Improving coiled coil stability while maintaining specificity by a bacterial hitchhiker selection system. J. Struct. Biol., 186, 335-348.
  • Einsle, O. (2014) Nitrogenase FeMo cofactor: An atomic structure in three simple steps. J. Biol. Inorg. Chem., 19, 737-745.

 

2013

  • Lucas, X., Wohlwend, D., Hügle, M., Schmidkunz, K., Gerhardt, S., Schüle, R., Jung, M., Einsle, O. & Günther, S. (2013) 4-Acyl Pyrroles: Mimicking Acetylated Lysines in Histone Code Reading. Angew. Chem. Intl. Ed., 52, 14055-14059.
  • Schlesier, J., Siegrist, J., Gerhardt, S., Erb, A., Blaesi, S., Richter, M., Einsle, O. & Andexer, J.N. (2013) Structural and functional characterization of the methionine adenosyltransferase form Thermococcus kodakarensis. BMC Struct. Biol., 13, 22. 
  • Zhang, L., Kaiser, J., Meloni, G., Yang, K.Y., Spatzal, T., Andrade, S.L.A., Einsle, O., Howard, J. & Rees, D.C. (2013) The 16th Fe in the Nitrogenase MoFe-Protein. Angew. Chem. Intl. Ed., 52, 10529-10532. 

  • Andrade, S.L.A. & Einsle, O. (2013) The Tricky Task of Nitrate/Nitrite Antiport. Angew. Chem. Intl. Ed., 52, 10422-10424.

  • Seidel, J., Schmitt, G., Hoffmann, M., Jendrossek, D. & Einsle, O. (2013) Structure of the processive rubber oxygenase RoxA from Xanthomonas sp. Proc. Natl. Acad. Sci. USA, 110, 13833-13838.

  • Spatzal, T., Einsle, O. & Andrade, S.L.A. (2013) Analysis of the Magnetic Properties of Nitrogenase FeMo Cofactor by Single-Crystal EPR Spectroscopy. Angew. Chem. Intl. Ed., 52, 10116-10119. 

  • Lü, W., Du, J., Schwarzer, N.J., Wacker, T., Andrade, S.L.A. & Einsle, O. (2013) The Formate/Nitrite Transporter family of anion channels.  Biol. Chem., 394, 715-727.

  • Friedrich, T. & Einsle, O. (2013) Highlight: European BioEnergetics Conference 2012 in Freiburg.  Biol. Chem., 394, 577-578.

  • Cavazzini, D., Meschi, F., Corsini, R., Bolchi, A., Rossi, G.L., Einsle, O. & Ottonello, S. (2013) Autoproteolytic activation of a symbiose-regulated truffle phospholipase A2.  J. Biol. Chem., 288, 1533-1547.

 

 2012 

  • Stolfa, D.A., Einsle, O., Sippl, W. & Jung, M. (2012) Current trends in epigenetic drug discovery.  Future Med. Chem., 4, 2029-2037.

  • Wüst, A., Schneider, L., Pomowski, A., Zumft, W. G., Kroneck, P. M. H. & Einsle, O. (2012) Nature’s way of handling a greenhouse gas: The copper-sulfur cluster of purple nitrous oxide reductase.  Biol. Chem., 393, 1067-1077.

  • Lü, W., Schwarzer, N.J., Du, J., Gerbig-Smentek, E., Andrade, S.L.A. & Einsle, O. (2012) Structure and mechanism of the nitrite channel NirC from Salmonella typhimurium.  Proc. Natl. Acad. Sci. USA, 109, 18395-18400.

  • Hermann, B., Kemper, F., Braun, M., Netzer, S., Dietrich, M., Kern, M., Simon, J., Wohlwend, D. & Einsle, O. (2012) Structure of a novel octaheme cytochrome c from Campylobacter concisus.  BBA-Bioenergetics, 1817, S156.

  • Morina, K., Schulte, M., Jurkovic, S., Burschel, S., Einsle, O & Friedrich, T. (2012) ROS production by E. coli respiratory complex I.  BBA-Bioenergetics, 1817, S59.

  • Vranas, M., Einsle, O. & Friedrich, T. (2012) Overproduction of Aquifex aeolicus complex I in E. coli nuo deletion strains.  BBA-Bioenergetics, 1817, S62-S63.

  • Friedrich, T., Einsle, O. & Gräber, P. (2012) Combining the multiple facets of bioenergetics.  Biochim. Biophys. Acta, 1817, 1709-1710.

  • Lü, W., Du, J., Schwarzer, N.J., Gerbig-Smentek, E., Einsle, O. & Andrade, S.L.A. (2012) The formate channel FocA exports the products of mixed-acid fermentation.  Proc. Natl. Acad. Sci. USA, 109, 13254-13259.

  • Friedrich, T., Hellwig, P. & Einsle, O. (2012) On the mechanism of respiratory complex I. In: A Structural Perspective on Respiratory Complex I: Structure and Function of NADH:ubiquinone oxidoreductase (Sazanov, L., ed.) Springer, Dodrecht.

  • Einsle, O. (2012) Enzyme or Electrode?  Structure, 20, 1132-1134.

  • Guttenberg, G., Hornei, S., Jank, T., Schwan, C., Lü, W., Einsle, O., Papatheodorou, P. & Aktories, K. (2012) Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.  J. Biol. Chem., 287, 24929-24940.

  • Speck, J., Hecky, J., Tam, H.K., Arndt, K.M. Einsle, O. & Müller, K.M. (2012) Exploring the Molecular Linkage of Protein Stability Traits for Enzyme Optimization by Iterative Truncation and Evolution.  Biochemistry, 51, 4850-4867.

  • Seidel, J., Hoffmann, M., Ellis, K.E., Seidel, A., Spatzal, T., Gerhardt, S., Elliott, S.J. & Einsle, O. (2012) MacA is a second cytochrome c Peroxidase in Geobacter sulfurreducens.  Biochemistry, 51, 2747-2456.

 

2011

  • Simon, J., Kern, M., Hermann, B., Einsle, O. & Butt, J.N. (2011) Physiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling.  Biochem. Soc. Transact., 39, 1864-1870.

  • Spatzal, T., Aksoyoglu, M., Zhang, L., Andrade, S.L.A., Schleicher, E., Weber, S., Rees, D.C. & Einsle, O. (2011) Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor.  Science, 334, 940.

  • Du, J., Say, R.F., Lü, W., Fuchs, G. & Einsle, O. (2011) Active site remodeling in the bifunctional fructose-6-bisphosphate aldolase/phosphatase. Nature, 478, 534-537. 

  • Pomowski, A., Zumft, W.G., Kroneck, P.M.H. & Einsle, O. (2011) N2O binding at a [4Cu:2S] copper-sulphur cluster in nitrous oxide reductase. Nature, 477, 234-237.

  • Schütz, B., Seidel, J., Sturm, G., Einsle, O. & Gescher, J. (2011) Investigation of the electron transport chain to and the catalytic activity of the diheme cytochrome c peroxidase CcpA of Shewanella oneidensis. Appl. Environ. Microbiol., 77, 6172-6180.

  • Ellis, K.E., Seidel, J., Einsle, O. & Elliott, S.J. (2011) Geobacter sulfurreducens cytochrome c peroxidases: Eletrochemical classifications of catalytic mechanisms. Biochemistry, 50, 4513-4520.

  • Einsle, O. (2011) Structure and function of formate-dependent cytochrome c nitrite reductase.  Meth. Enzymol., 496, 399-422.

  • Lü, W., Du, J., Wacker, T., Gerbig-Smentek, E., Andrade, S.L.A. & Einsle, O.(2011) pH-dependent gating in a FocA formate channel.  Science, 332, 352-354.

  • Guttenberg, G., Papatheodorou, P., Genisyuerek, S., Lü, W., Jank, T., Einsle, O. & Aktories, K. (2011) Inositol hexakisphosphate-dependent processing of Clostridium sordellii lethal toxin and Clostridium novyi alpha toxin.  J. Biol. Chem., 286, 14779-14786.

  • Alagaratnam, S, Meeuwenoord, M.J., Navarro, J.A., Hervás, M., De la Rosa, M.A., Hoffmann, M., Einsle, O., Ubbink, M. & Canters, G.W. (2011) Probing the reactivity of different forms of azurin by flavin photoreduction.  FEBS J., 278, 1506-1521. 

  • Litz, C., Helfmann, S., Gerhardt, S. &  Andrade, S.L.A. (2011). Structure of GlnK1, a signaling protein from Archaeoglobus fulgidus.  Acta Crystallogr., F67, 178-181.


2005 - 2010

  • Pomowski, A., Zumft, W.G., Kroneck, P.M.H. & Einsle, O. (2010) Crystallization of purple nitrous oxide reductase from Pseudomonas stutzeri. Acta. Crystallogr., F66, 1541-1543.

  • Buttar, D., Colclough, N., Gerhardt, S., Macfaul, P.A., Philipps, S.D., Plowright, A., Whittamore, P., Tam, K., Maskos, K., Steinbacher, S. & Steuber, H. (2010) A combined spectroscopic and crystallographic approach to probing drug-human serum albumin interactions.  Bioorg Med Chem., 18, 7486-7496.

  • Lü, W., Du, J., Stahl, M., Tzivelekidis, T., Belyi, Y., Gerhardt, S., Aktories, K. & Einsle, O. (2010) Structural basis of the action of glucosyltransferase Lgt1 from Legionella pneumophila.  J. Mol. Biol., 396, 321-331.

  • Helfmann, S., Lü, W., Litz, C., Andrade, S.L.A. (2010) Cooperative binding of MgATP and MgADP in the trimeric PII protein GlnK2 from Archaeoglobus fulgidus.  J. Mol. Biol., 402, 402, 165-177.

  • Asaad, N., Bethel, P.A., Coulson, M.D., Dawson, J.E., Ford S.J., Gerhardt, S., Grist, M, Hamlin, G.A., James, M.J., Jones, E.V., Karoutchi, G.I., Kenny, P.W., Morley, A.D., Oldham, K., Rankine, N., Ryan, D., Wells, S.L., Wood, L., Augustin, M., Krapp, S., Simader, H. & Steinbacher, S. (2009) Dipeptidyl nitrile inhibitors of Cathepsin L., Bioorg Med Chem Lett., 19, 4280-4283.

  • Bethel, P.A., Gerhardt, S., Jones, E.V., Kenny, P.W., Karoutchi, G.I., Morley, A.D., Oldham, K., Rankine, N., Augustin, M., Krapp, S., Simader, H. & Steinbacher, S. (2009) Design of selective Cathepsin Inhibitors., Bioorg Med Chem Lett., 19, 4622-4625.

  • Gerhardt, S., Abbott, W.M., Hargreaves, D., Pauptit, R.A., Davies, R.A., Needham, M.R., Langham, C., Barker, W., Aziz, A., Snow, M.J., Dawson, S., Welsh, F., Wilkinson, T., Vaugan, T., Beste, G., Bishop, S., Popovic, B., Rees, G., Sleeman, M., Tuske, S.J., Coales, S.J., Hamuro, Y. & Russell, C. (2009) Structure of IL-17A in complex with a potent, fully human neutralizing antibody., J. Mol. Biol.,  394, 905-921.

  • Hoffmann, M., Seidel, J. & Einsle, O. (2009) CcpA from Geobacter sulfurreducens is a Basic Di-heme Cytochrome c Peroxidase., J. Mol. Biol., 393, 951-965. 

  • Kohlstädt, M., Dörner, K., Labatzke, R., Koç, C., Hielscher, R., Schiltz, E., Einsle, O., Hellwig, P. & Friedrich, T. (2008) Heterologous Production, Isolation, Characterization and Crystallization of a Soluble Fragment of the NADH:Ubiquinone Oxidoreductase (Complex I) from Aquifex aeolicus.
Biochemistry, 47, 13036-13045.

  • Heitmann, D. & Einsle, O. (2008) Pseudo-merohedral twinning in crystals of the diheme c-type cytochrome DHC2 from Geobacter sulfurreducens.  Acta Crystallogr., D64, 993-999.

  • Seiffert, G. B., Abt, D., ten Brink, F., Fischer, D., Einsle, O. & Kroneck, P. M. H. (2008)  Acetylene Hydratase.
In: Handbook of Metalloproteins (Messerschmidt, A., ed.) John Wiley & Sons, New York.

  • Andrade, S. L., Ribbe, M. W., Hu, Y. & Einsle, O. (2008) Recent Advances on Nitrogenase. In: Handbook of Metalloproteins (Messerschmidt, A., ed.) John Wiley & Sons, New York.

  • Meyer, J., Andrade, S. L.  & Einsle, O. (2008) Thioredoxin-like [2Fe:2S] Ferredoxin. In: Handbook of Metalloproteins (Messerschmidt, A., ed.) John Wiley & Sons, New York.

  • Lukat, P., Hoffmann, M. & Einsle, O. (2008) Crystal packing of the c6-type cytochrome OmcF from Geobacter sulfurreducens is mediated by an N-terminal Strep-tag II. 
Acta Crystallogr., D64, 919-926.

  • Kern, M., Einsle, O. & Simon, J. (2008) Variants of the tetrahaem cytochrome c quinol dehydrogenase NrfH characterize the menaquinol binding site, the haem c binding motifs and the transmembrane segment.
 Biochem. J., 414, 73-79.

  • Cavalieri, C., Biermann, N., Vlasie, M. D., Einsle, O., Merli, A., Ferrari, D., Rossi, G.-L. & Ubbink, M. (2008) Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus. 
Biochemistry, 47, 6560-6570.

  • Ahuja, U., Rozhkova, A., Glockshuber, R., Thöny-Meyer, L. & Einsle, O. (2008) Helix Swapping Leads to Dimerization of the N-terminal Domain of the c-type Cytochrome Maturation Protein CcmH from Escherichia coli. 
FEBS Lett., 582, 2779-2786. 

  • Hoffmann, M., Braaz, R., Jendrossek, D. & Einsle, O. (2008) Crystallization of the extracellular rubber oxygenase RoxA from Xanthomonas sp. Strain 35Y. 
Acta Crystallogr., F64, 123-125.

  • Lukat, P., Rudolf, M., Stach, P., Messerschmidt, A., Kroneck, P. M. H., Simon, J. & Einsle, O. (2008) Binding and Reduction of Sulfite by Cytochrome c Nitrite Reductase. 
Biochemistry, 47, 2080-2086.

  • Andrade, S. L. A., Patridge, E. V., Ferry, J. G. & Einsle, O. (2007) Crystal Structure of the NADH:Quinone Oxidoreductase WrbA from Escherichia coli.
J. Bacteriol., 189, 9101-9107.

  • Seiffert, G. B., Ullmann, G. M., Messerschmidt, A., Schink, B., Kroneck, P. M. H. & Einsle, O. (2007) Structure of the Non Redox-Active Tungsten / [4Fe:4S] Enzyme Acetylene Hydratase. 
Proc. Natl. Acad. Sci. USA, 104, 3073-3077.

  • Einsle, O., Andrade, S. L., Dobbek, H., Meyer, J. & Rees, D. C. (2007) Assignment of Individual Metal Redox States in a Metalloprotein by Crystallographic Refinement at Multiple X-ray Wavelengths. 
J. Am. Chem. Soc., 129, 2210-2211.

  • Andrade, S. L. & Einsle, O. (2007) The Amt/Mep/Rh Family of Ammonium Transport Proteins. 
Mol. Memb. Biol., 24, 357-365.

  • de Jongh, T. E., Hoffmann, M., Einsle, O., Cavazzini, D., Rossi, G.-L., Ubbink, M. & Canters, G. W. (2007) Inter- and Intramolecular Electron Transfer in Modified Azurin Dimers. 
Eur. J. Inorg. Chem., 2007, 2627-2634.

  • Einsle, O., Seiffert, G., Sosa-Torres, M. E. & Kroneck, P. M. H. (2006) Bakterien sind die besten Chemiker. 
Biospektrum, 12, 346-349.

  • Andrade, S. L., Dickmanns, A., Ficner, R. & Einsle, O. (2005) Crystal Structure of the Archaeal Ammonium Transporter Amt-1 from Archaeoglobus fulgidus. 
Proc. Natl. Acad. Sci. USA, 102, 14994-14999.

  • Andrade, S. L., Dickmanns, A., Ficner, R. & Einsle, O. (2005) Expression, Purification and Crystallization of the Ammonium Transporter Amt-1 fromArchaeoglobus fulgidus. 
Acta Crystallogr., F61, 861-863.

  • Heitmann, D. & Einsle, O. (2005) Structural and Biochemical Characterization of DHC2, a Novel Diheme Cytochrome c from Geobacter sulfurreducens.
Biochemistry, 44, 12411-12419.

  • Andrade, S.L., Cruz, F., Drennan, C. L., Ramakrishnan, V., Rees, D. C., Ferry, J. G. & Einsle, O. (2005) Structures of the Iron-Sulfur Flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus. 
J. Bacteriol., 187, 3848-3854.

  • Rees, D. C., Tezcan, F. A., Haynes, C. A., Walton, M. Y., Andrade, S. L., Einsle, O. & Howard, J. B. (2005) Structural Basis of Nitrogen Fixation. 
Philos. Transact. A Math. Phys. Eng. Sci., 363, 971-984.

  • Einsle, O., Niessen, H., Abt, D. J., Seiffert, G., Schink, B., Huber, R., Messer-schmidt, A. & Kroneck, P. M. H. (2005) Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase from Pelobacter acetylenicus. 
Acta Cryst., F61, 299-301.

  • Fritz, G., Einsle, O., Rudolf, M., Schiffer, A. & Kroneck, P. M. H.  (2005) Key Bacterial Multi-Centered Metal Enzymes Involved in Nitrate and Sulfate Respiration. 
J. Mol. Microbiol. Biotechnol., 10, 223-233.

  • Corbett, M. C., Tezcan, F. A., Einsle, O., Walton, M. Y., Rees, D. C. Latimer, M. J., Hedman, B. & Hodgson, K. O. (2005) Mo K- and L-edge X-ray absorption spectroscopic study of the ADP-AlF4- stabilized nitrogenase complex: Comparison with MoFe protein in solution and single crystal. 
J. Synchrotron Rad., 12, 28-34.


Older Publications

  • Einsle, O. & Kroneck, P. M. H. (2004) Structural Basis of Denitrification. 
Biol.Chem., 385, 875-883.

  • Messerschmidt, A., Niessen, H., Abt, D., Einsle, O., Schink, B. & Kroneck, P. M. H. (2004) Crystal structure of pyrogallol-phloroglucinol transhydroxylase, a Mo enzyme capable of intermolecular hydroxyl transfer between phenols.
Proc. Natl. Acad. Sci. USA, 101, 11571-11576.

  • Simon, J., Einsle, O, Kroneck, P. M. H. & Zumft, W.G. (2004) The unprecedented nos gene cluster of Wolinella succinogenes encodes a novel respiratory electron transfer pathway to cytochrome c nitrous oxide reductase.
FEBS Lett., 569, 7-12.

  • Schmid, B., Einsle, O., Willing, A., Yoshida, M., Howard, J. & Rees, D. C. (2002) Biochemical and structural characterization of the crosslinked complex of nitrogenase: com-parison to the ADP-AlF4--stabilized structure.
Biochemistry, 41, 15557-15565.

  • Einsle, O., Messerschmidt, A., Huber, R., Kroneck, P. M. H. & Neese, F. (2002) Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase. 
J. Am. Chem. Soc., 124, 11737-11745.

  • Einsle, O., Tezcan, F. A., Andrade, S. L., Schmid, B., Yoshida, M., Howard, J. B. & Rees, D. C. (2002) Nitrogenase MoFe protein at 1.16 Å resolution: A central ligand in the FeMo cofactor. 
Science, 297, 1696-1700.

  • Yeh, A. P., Ambroggio, X. I., Andrade, S. L., Einsle, O., Chatelet, C., Meyer, J. & Rees, D. C. (2002) High resolution crystal structures of the wild type and Cys-55→Ser and Cys-59→Ser variants of the Thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. 
J. Biol. Chem., 277, 34499-34507.

  • Rudolf, M., Einsle, O., Neese, F. & Kroneck, P. M. H. (2002) Pentahaem cytochrome c nitrite reductase: reaction with hydroxylamine, a potential reaction intermediate and substrate. 
Biochem. Soc. Transact., 30, 649-653.

  • Schmid, B., Ribbe, M. W., Einsle, O., Yoshida, M., Thomas, L. M., Rees, D. C. & Burgess, B. K. (2002) Implications for metalloprotein assembly from the structure of a FeMo cofactor deficient nitrogenase MoFe protein. 
Science, 296, 352-356.

  • van Amsterdam, I. M. C., Ubbink, M., Einsle, O., Messerschmidt, A., Merli, A., Cavazzini, D., Rossi, G. L. & Canters, G. W. (2002) Dramatic modulation of electron transfer in protein crystals by crosslinking. 
Nature Struct. Biol., 9, 48-52.

  • Abt, D. J., Einsle, O., Niessen, H., Krieger, R., Messerschmidt, A., Schink, B. & Kroneck, P. M. H. (2002) Crystallization and preliminary X-ray analysis of the molybdenum-dependent pyrogallol-phloroglucinol transhydroxylase ofPelobacter acidigallici. 
Acta Crystallogr., D58, 343-345.

  • Einsle, O., Stach, P., Messerschmidt, A., Klimmek, O., Simon, J., Kröger, A. & Kroneck, P. M. H. (2002) Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) fromWolinella succinogenes. 
Acta Crystallogr., D58, 341-342.

  • van Amsterdam, I. M. C., Ubbink, M., Jeuken, L. J. C., Verbeet, M. P., Einsle, O., Messerschmidt, A. & Canters, G. W. (2001) Effects of dimerization on protein electron transfer. 
Chem. Eur. J., 7, 2390-2406.

  • Einsle, O. (2001) Cytochrome c nitrite reductase.  In: Handbook of Metalloproteins (Messerschmidt, A., Huber, R., Wieghardt, K. & Poulos, T., eds.). John Wiley & Sons, NewYork.

  • Einsle, O., Foerster, S., Mann, K. H., Fritz, G., Messerschmidt, A. & Kroneck, P. M. H. (2001) Spectroscopic investigation, reactivity and structure determination of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6. 
Eur. J. Biochem., 268, 3028-3035.

  • Simon, J., Gross, R., Einsle, O., Kroneck, P. M. H., Kröger, A. & Klimmek, O.(2000) A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes. 
Mol. Microbiol., 35, 686-696.

  • Einsle, O., Stach, P., Messerschmidt, A., Simon, J., Kröger, A., Huber, R. & Kroneck, P. M. H. (2000) Cytochrome c nitrite reductase from Wolinella succinogenes: Structure at 1.6 Å resolution, inhibitor binding and heme-packing motifs. 
J. Biol. Chem., 275, 39608-39616.

  • Stach, P., Einsle, O., Schumacher, W., Kurun, E. & Kroneck, P. M. H. (2000) Bacterial cytochrome c nitrite reductase: new structural and functional aspects. 
J. Inorg. Biochem., 79, 381-385.

  • Einsle, O., Mehrabian, Z., Nalbandyan, R. & Messerschmidt, A. (2000) Crystal structure of plantacyanin, a basic blue cupredoxin from spinach. 
J. Biol. Inorg. Chem., 5, 666-672.

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