Dr. rer. nat. Matthias Stein, M.Sc.
Dr. rer. nat. Matthias Stein, M.Sc.
Phone: +49 391 6110 436
Fax: +49 391 6110 403



Currently there are no jobs available.


MSD-Group Publications


  • M. Mirmohades, S. Pullen, M. Stein, S. Maji, S. Ott, L. Hammarström, R. Lomoth. Direct Observation of Key Catalytic Intermediates in a Photoinduced Proton Reduction Cycle with a Diiron Carbonyl Complex. J. Am. Chem. Soc., 136, 17366-17369 (2014).

  • E. Edler, M. Stein. Spin-State-Dependent Properties of an Iron(III) Hydrogenase Mimic. European Journal of Inorganic Chemistry, 22, 3587-3599  (2014).

  • G. M. Chambers, J. Mitra, T.B. Rauchfuss, M. Stein. NiI/RuII Model for the Ni-L State of the [NiFe] Hydrogenases: Synthesis, Spectroscopy, and Reactivity. Inorganic Chemistry, 53, 4243-4249 (2014).

  • G. Chambers, R. Angamuthu, J. Mitra, T.B. Rauchfuss, M. Stein. Ni-Ru Dithiolates as Models for the Ni-L State in [NiFe]-Hydrogenase.  J. Biol. Inorg. Chem. 19, S519 (2014).

  • S. Yazdi, M. Andersson, F. Elinder, M. Stein, E. Lindahl. Molecular Characterization of the Binding of Polyunsaturated Fatty Acids to a Voltage-Gated Potassium Channel. Biophysical Journal, 106, 739a (2014).

  • S. Kaur-Ghumaan, M. Stein. [NiFe] Hydrogenases: How close do Structural and Functional Mimics Approach the Active Site? Dalton Transactions, 43, 9392-9405 (2014)

  • A. Orthaber, M. Karnahl, S. Tschierlei, D. Streich, M. Stein, S. Ott. Coordination and conformational isomers in mononuclear iron complexes with pertinence to the [FeFe] hydrogenase active site. Dalton Transactions, 43, 4537-4549 (2014). (New Talents Europe Special Issue).


  • M. Stein, S. Kaur-Ghumaan. Microbial hydrogen conversion in the presence of oxygen. Biochemical Society Transactions, 41, 1317-1324 (2013).
  • Ö. F. Erdem, M. Stein, S. Kaur-Ghumaan, E.J. Reijerse, S. Ott, W. Lubitz. Chemistry- A European Journal,19, 14566-14572 (2013).
  • W. Wang, M.J. Nilges, T.B. Rauchfuss, M. Stein. Isolation of a mixed-valence diiron hydride:evidence for a spectatot hydride in hydrogen evolution catalysis. Journal American Chemical Society, 135, 3633-3639 (2013).


  • D. Schilter, T.B. Rauchfuss, M. Stein. Connecting [NiFe]- and [FeFe]-Hydrogenases: Mixed-Valence Nickel-Iron Dithiolates with Rotated Structures. Inorganic Chemistry, 51, 8931-8941, (2012).
  • D. Schilter, M.J. Nilges, M. Chakrabarti, P.A. Lindahl, T.B. Rauchfuss, M. Stein. Mixed-valence nickel–iron dithiolate models of the [NiFe]-hydrogenase active site. Inorganic Chemistry51, 2338-2348, (2012). (Selected as Cover Illustration for Inorganic Chemistry)

  • M.-E. Pandelia, P. Infossi, M. Stein, M.-T. Giudici-Orticoni, Wolfgang Lubitz. Spectroscopic characterization of the key catalytic intermediate Ni–C in the O2-tolerant [NiFe] hydrogenase I from Aquifex aeolicus: evidence of a weakly bound hydride. Chem. Comm.48, 823-825, (2012).


  • Ö.F. Erdem, L. Schwartz, M. Stein, A. Silakov, S. Kaur-Ghumaan, P. Huang, S. Ott, E.J. Reijerse, W. Lubitz. A Model of the [FeFe] Hydrogenase Active Site with a Biologically Relevant Azadithiolate Bridge: A Spectroscopic and Theoretical Investigation. Angewandte Chemie International Edition50, 1439-1443, (2011).
  • Ö.F. Erdem, L. Schwartz, M. Stein, A. Silakov, S. Kaur-Ghumaan, P. Huang, S. Ott, E.J. Reijerse, W. Lubitz. Ein Modell des aktiven Zentrums der [FeFe]-Hydrogenasen mit biologisch relevanter Azadithiolat-Brücke: eine spektroskopische und theoretische Untersuchung Angewandte Chemie123, 1475-1479, (2011).
  • T. Goris, A.F. Wait, J. Fritsch, N. Heidary, M. Stein, I. Zebger, F. Lendzian, F.A. Armstrong, B. Friedrich, O. Lenz. A Unique Iron-Sulfur Cluster is Crucial for Oxygen Tolerance of a [NiFe]-Hydrogenase Nature Chemical Biology7, 310-318, (2011).
  • H. Kaemmerer, R. Zinke, H. Lorenz, M. J. Jones, A. Seidel-Morgenstern, M. Stein. Corrigendum to: Selective crystallisation of a chiral compound-forming system- Solvent screening, SLE determination and process design Fluid Phase Equilibria307, 110-112, (2011).
  • M. Stein. Commentary on "A Nickel(II)-Based Radical-Ligand Complex as a Functional Model of Hydrogenase". Chemistry- A European Journal17, 15046-15048.
  • J. Fritsch, S. Löscher, O. Sanganas, E. Siebert, I. Zebger, M. Stein, M. Ludwig, A. L. de Lacey, H. Dau, B. Friedrich, O. Lenz, M. Haumann. [NiFe]- and [FeS]-cofactors in the membrane-bound hydrogenase of Ralstonia eutropha investigated by X-ray absorption spectroscopy: insights into O2-tolerant H2-cleavage. Biochemistry50, 5858-5869, (2011).
  • R. ZinkeM. Stein. Enantioselective Crystallization Process Design From Predictive COSMO Calculations. In:Conference Proceedings of the 2011 AIChE Annual Meeting, 190x, Omnipress, New York, ISBN 978-0-8169-1070-0.


  • M. Stein, R.R. Gabdoulline, R.C. Wade. Cross-Species Analysis of the Glycolytic Pathway by Comparison of Molecular Interaction Fields. Molecular BioSystems6, 162-174, (2010).
  • S. Löscher, A. Gebler, M. Stein, O. Sanganas, T. Buhrke, I. Zebger, H. Dau, B. Friedrich, O. Lenz, M. Haumann. Protein-Protein Complex Formation Affects the Ni-Fe and Fe-S Centers in the H2-Sensing Regulatory Hydrogenase from Ralstonia eutropha H16. ChemPhysChem11, 1297-1306, (2010).
  • S. Kaur-Ghumann, L. Schwartz, R. Lomoth, M. Stein, S. Ott. Catalytic Hydrogen Evolution from Mononuclear Iron(II) Carbonyl Complexes as Minimal Functional Models of the [FeFe] Hydrogenase Active Site. Angewandte Chemie International Edition49, 8033-8036, (2010).
  • S. Kaur-Ghumann, L. Schwartz, R. Lomoth, M. Stein, S. Ott. Katalytische Wasserstofferzeugung an einem einkernigen Eisen(II)-Carbonylkomplex als kleinstes funktionelles Modell für das aktive Zentrum von [FeFe]-Hydrogenasen. Angewandte Chemie122, 8207-8211, (2010).


  • C. Müller, M. A. Gomez-Zurita Frau, D. Ballinar, S. Colombo, A. Bitto, E. Martegani, C. Airoldi, A. S. van Neuren, M. Stein, J. Weiser, C. Battistini, F. Peri
    Design, Synthesis, and Biological Evaluation of Levoglucosenone-Derived Ras Activation Inhibitors. ChemMedChem,4, 524-528, (2009).
  • P. S. Singh, H. C. Rudbeck, P. Huang, S. Ezzaher, L. Eriksson, M. Stein, S. Ott, R. Lomoth. (I,0) Mixed-Valence State of a Diiron Complex with Pertinence to the [FeFe]-Hydrogenase Active Site: An IR, EPR, and Computational Study. Inorganic Chemistry48, 10883-10885, (2009).


  • M. Stein, R. R. Gabdoulline, R. C. Wade. Calculating enzyme kinetic parameters from protein structures. Biochem. Soc. Trans.36, 51-54, (2008).
  • S. Richter, A. Wenzel, M. Stein, R. R. Gabdoulline, R. C. Wade. WebPIPSA: A Web Server for the Comparison of Protein Interaction Properties. Nucleic Acids Research36, W276-W280, (2008).
  • A. Weidemann, S. Richter, M. Stein, S. Sahle, R. Gauges, R. R. Gabdoulline, I. Surovtsova, N. Semmelrock, B. Besson, I. Rojas, R. C. Wade, U. Kummer
    SYCAMORE - a Systems Biology Computational Analysis and Modeling Research Environment. Bioinformatics24, 1463-1464, (2008).


  • M. Stein, R. Gabdoulline, R. C. Wade. The Estimation of Kinetic Parameters in Systems Biology by Comparing Molecular Interaction Fields of Enzymes
    In: Experimental Standard Conditions on Enzyme Characterization, 2nd International Beilstein Workshop, M. G. Hicks, C. Kettner (eds.), Logos Verlag, Berlin, 237-254, (2007).
  • M. Stein, R. R. Gabdoulline, R. C. Wade. Bridging from Molecular Simulation to Biochemical Networks. Curr. Op. Struct. Biol.17, 166-172, (2007).
  • R. R. Gabdoulline, M. Stein, R. C. Wade. qPIPSA: Relating Enzymatic Kinetic Parameters and Interaction Fields. BMC Bioinformatics8, 373, (2007).
  • G. Eilers, L. Schwartz, M. Stein, G. Zampella, L. de Gioia,S. Ott, R. Lomoth. Ligand vs. Metal Protonation of an Iron Hydrogenase Active Site Mimic. Chemistry – A European Journal, 13, 7075-7084, (2007).
  • S. Löscher, L. Schwartz, M. Stein, S. Ott, M. Haumann. Facilitated Hydride Binding in an Fe-Fe Hydrogenase Active-Site Biomimic Revealed by X-ray Absorption Spectroscopy and DFT Calculations. Inorganic Chemistry, 46, 11094-11105, (2007).


  • M. van Gastel, M. Stein, M. Brecht, O. Schröder , F. Lendzian, R. Bittl, H. Ogata, Y. Higuchi, W.Lubitz
    A Single-Crystal ENDOR and Density Functional Theory Study of the Oxidized States of the [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Biol. Inorg. Chem. 11, 41-51, (2006).
  • M. van Gastel, M. Stein, M. Brecht, O. Schröder , F. Lendzian, R. Bittl, H. Ogata, Y. Higuchi, W.Lubitz. A Single-Crystal ENDOR and Density Functional Theory Study of the Oxidized States of the [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Biol. Inorg. Chem. 11, 41-51, (2006).
  • M. Stein, R. Gabdoulline, R. C. Wade. Integrating Structural and Kinetic Enzymatic Information in Systems Biology. In: Proceedings of the NIC Workshop “From Computational Biophysics to Systems Biology”NIC Series34, 129-132, (2006).


  • A. Ragusa, S. Rossi, J.M. Hayes, M. Stein, J.D. Kilburn. Novel Enantioselective Receptors for N-Protected Glutamate and Aspartate. Chemistry – A European Journal11, 5674-5688, (2005).
  • F. Peri, C. Airoldi, S. Colombo, E. Martegani, A. S. van Neuren, M. Stein, C. Marinzi, F. Nicotra. Design, Synthesis and Biological Evaluation of Sugar-Derived Ras Inhibitors. ChemBioChem,6, 1839-1848, (2005).


  • M. Bruschi, L. de Gioia, G. Zampella, M. Reiher, P. Fantucci, M. Stein. A Theoretical Study of Spin States in Ni-S4 Complexes and Models of the [NiFe] Hydrogenase Active Site. J. Biol. Inorg. Chem. 9, 873-884, (2004).
  • J. M. Hayes, M. Stein, J. Weiser. Accurate Calculations of Ligand Binding Free Energies: Chiral Separation with Enantioselective Receptors. J. Phys. Chem. A 108, 3572-3580, (2004).
  • A. del Rio, J.M. Hayes, M. Stein, P. Piras, C. Roussel. Theoretical Reassessment of Whelk-O1 as an Enantioselective Receptor for 1-(4-halogeno-phenyl)-1-ethylamine Derivatives. Chirality 16, S1-S11, (2004).
  • M. Stein, W. Lubitz. Relativistic DFT Calculation of the Reaction Cycle Intermediates of [NiFe] Hydrogenase: A Contribution to Understanding the Enzymatic Mechanism. J. Inorg. Biochem. 98, 862-877, (2004).


  • S. Foerster, M. Stein, M. Brecht, Y. Higuchi, W. Lubitz. Single Crystal EPR Studies of the Reduced Active Site of NiFe]-Hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Am. Chem. Soc.123, 83-93, (2003).
  • W Lubitz, M. Brecht, S. Foerster, M. van Gastel, M. Stein. ESR and ENDOR Studies of [NiFe] Hydrogenase: Contributions to Understanding the Mechanism of Biological Hydrogen Conversion. In: ACS Symposium Series No. 858: Paramagnetic Resonance of Metallobiomolecules, J. Telser (Ed.), Chapter 7, (2003).


  • M.Stein, W. Lubitz. Quantum Chemical Calculations of [NiFe] Hydrogenase. Curr. Op. Chem. Biol.6, 243-249, (2002).
  • W. Lubitz, M. Brecht, S. Foerster, M. Stein, Y. Higuchi, T. Buhrke, B. Friedrich. EPR and Theoretical Investigations of [NiFe] Hydrogenase: Insight into the Mechanism of Biological Hydrogen Conversion. In: EPR in the 21st Century: Basics and Applications to Material, Life and Earth Sciences; A. Kawamori, J. Yamauchi and H. Ohta (eds.), Elsevier Publisher, 437-445, (2002).


  • M. Stein, E. van Lenthe, E. J. Baerends, W. Lubitz. g-and A-Tensor Calculations in the Zero-Order Approximation for Relativistic Effects of Ni-Complexes Ni(mnt)2- and Ni(CO)3H as Model Complexes for the. Active Center of [NiFe]-Hydrogenase. J. Phys. Chem. A105, 416-425, (2001).
  • M. Stein E. van Lenthe, E. J. Baerends, W. Lubitz. Relativistic DFT Calculations of the Paramagnetic Intermediates of [NiFe] Hydrogenase. Implications for the Enzymatic Mechanism. J. Am. Chem. Soc.123, 5839-5840, (2001).
  • M. Stein, W. Lubitz. DFT Calculations of the Electronic Structure of the Paramagnetic States Ni-A, Ni-B and Ni-C of [NiFe] Hydrogenase. Phys. Chem. Chem. Phys.3, 2668-2675, (2001).
  • M. Stein , W. Lubitz. Characterization of the Paramagnetic Intermediates of [NiFe] Hydrogenase by means of Relativistic DFT Calculations. J. Inorg. Biochem.86, 442, (2001).
  • M. Stein. DFT- A Promising Tool for Studying Transition Metal Enzymes. In: Hydrogen as a Fuel, R. Cammack and R. L. Robson (Eds.); Taylor and Francis, 154-158, (2001).
  • C. Teutloff, R. Bittl, M. Stein, P. Jordan, N. Krauß, W. Lubitz. Structure-based Analysis of the Magnetic Resonance Parameters of the Phylloquinone Acceptor A1 in PS I. In: PS2001 - Proceedings of the 12th International Congress on Photosynthesis, CSIRO Publishing, Melbourne, Australia, (2001).
  • C. Teutloff, W. Hofbauer, S. G. Zech, M. Stein, R. Bittl, W. Lubitz. High Frequency EPR Studies on Cofactor Radicals in Photosystem I. Appl. Mag. Res.21, 363-379, (2001).


  • O. Trofanchuk, M. Stein, Ch. Gessner, F. Lendzian, Y. Higuchi, W. Lubitz. Single Crystal EPR Studies of the Oxidized Active Site of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Biol. Inorg. Chem.5, 36-44, (2000).
  • W. Lubitz, M. Stein, M. Brecht, O. Trofanchuk, S. Foerster, Y. Higuchi, E. van Lenthe, F. Lendzian. Single Crystal EPR and DFT Studies of the Paramagnetic States of [NiFe] Hydrogenase fromDesulfovibrio vulgarisBiophys. J.78 A, 1660, (2000).
  • R. Isaacson, F. Lendzian, M. Stein, W. Lubitz, C. Boullais. Identification of ENDOR Lines in QA-and QB- in RCs of Rb. sphaeroides by Selective Isotopic Labeling. Biophys. J. , 78 A , 2001, (2000).
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