Wolfgang Lubitz

Max Planck Institute for Chemical Energy Conversion, Mülheim-on-Ruhr, North Rhine-Westphalia, Germany

Are you Wolfgang Lubitz?

Claim your profile

Publications (402)1905.71 Total impact

  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: The symmetry of the arrangement of objects has fascinated philosophers, artists and scientists for a long time, and still does. Symmetries often exist in Nature, but is also created artificially, for instance by chemical synthesis of novel molecules and materials. The one-sided, non-orientable Möbius band topology is a paradigm of such a symmetry-based fascination. In the early 1960’s, in synthetic organic chemistry the interest in molecules with Möbius symmetry was greatly stimulated by a short paper by Edgar Heilbronner. He predicted that sufficiently large [n]annulenes with a closed-shell electron configuration of 4n π-electrons should allow for sufficient π-overlap stabilization to be synthesizable by twisting them with a 180◦ phase change into the Möbius symmetry of their hydrocarbon skeleton. In 2007, the group of Lechosław Latos-Grażyński succeeded in synthesizing the compound di-p-benzi[28]hexa-phyrin(1.1.1.1.1.1), compound 1, which can dynamically switch between Hückel and Möbius conjugation depending, in a complex manner, on the polarity and temperature of the surrounding solvent. This discovery of “topology switching” between the two-sided (Hückel) and one-sided (Möbius) molecular state with closed-shell electronic configuration was based primarily on the results of NMR spectroscopy and DFT calculations. The present EPR and ENDOR work on the radical cation state of compound 1 is the first study of a ground-state open-shell system which exhibits a Hückel-Möbius topology switch that is controlled by temperature, like in the case of the closed-shell precursor. The unpaired electron interacting with magnetic nuclei in the molecule is used as a sensitive probe for the electronic structure and its symmetry properties. For a Hückel conformer with its higher symmetry, we expect – and observe – fewer ENDOR lines than for a Möbius conformer. The ENDOR results are supplemented by and in accordance with theoretical calculations based on density functional theory at the ORCA level.
    Physical Chemistry Chemical Physics 02/2015; 17(9). DOI:10.1039/C4CP05745G · 4.20 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: [FeFe]-hydrogenases are to date the only enzymes for which it has been demonstrated that the native inorganic binuclear cofactor of the active site Fe2(adt)(CO)3(CN)2 (adt = azadithiolate = [S-CH2-NH-CH2-S](2-)) can be synthesized on the laboratory bench and subsequently inserted into the unmaturated enzyme to yield fully functional holo-enzyme (Berggren, G. et al. (2013) Nature 499, 66?70, Esselborn, J. et al. (2013) Nat Chem Biol 9, 607?610). In the current study, we exploit this procedure to introduce non-native cofactors into the enzyme. Mimics of the binuclear sub-cluster with a modified bridging dithiolate ligand (thiodithiolate, N-methylazadithiolate, dimethyl-azadithiolate) and three variants containing only one CN(-) ligand were inserted into the active site of the enzyme. We investigate the activity of these variants for hydrogen oxidation as well as proton reduction and their structural accommodation within the active site was analyzed using Fourier transform infrared spectroscopy. Interestingly, the mono-cyanide variant with the azadithiolate bridge showed ?50% of the native Enzyme activity. This would suggest that the CN(-) ligands are not essential for catalytic activity but rather serve to anchor the binuclear subsite inside the protein pocket through hydrogen bonding. The inserted artificial cofactors with a propanedithiolate and an N-methylazadithiolate bridge as well as their mono-cyanide variants also showed residual activity. However, these activities were less than 1% of the native enzyme. Our findings indicate that even small changes in the dithiolate bridge of the binuclear sub-site lead to a rather strong decrease of the catalytic activity. We conclude that both the Br?nsted base function and the conformational flexibility of the native azadithiolate amine moiety are essential for the high catalytic activity of the native enzyme.
    Biochemistry 01/2015; DOI:10.1021/bi501391d · 3.38 Impact Factor
  • Hideaki Ogata, Koji Nishikawa, Wolfgang Lubitz
    [Show abstract] [Hide abstract]
    ABSTRACT: The enzyme hydrogenase reversibly converts dihydrogen to protons and electrons at a metal catalyst. The location of the abundant hydrogens is of key importance for understanding structure and function of the protein. However, in protein X-ray crystallography the detection of hydrogen atoms is one of the major problems, since they display only weak contributions to diffraction and the quality of the single crystals is often insufficient to obtain sub-ångström resolution. Here we report the crystal structure of a standard [NiFe] hydrogenase (∼91.3 kDa molecular mass) at 0.89 Å resolution. The strictly anoxically isolated hydrogenase has been obtained in a specific spectroscopic state, the active reduced Ni-R (subform Ni-R1) state. The high resolution, proper refinement strategy and careful modelling allow the positioning of a large part of the hydrogen atoms in the structure. This has led to the direct detection of the products of the heterolytic splitting of dihydrogen into a hydride (H(-)) bridging the Ni and Fe and a proton (H(+)) attached to the sulphur of a cysteine ligand. The Ni-H(-) and Fe-H(-) bond lengths are 1.58 Å and 1.78Å, respectively. Furthermore, we can assign the Fe-CO and Fe-CN(-) ligands at the active site, and can obtain the hydrogen-bond networks and the preferred proton transfer pathway in the hydrogenase. Our results demonstrate the precise comprehensive information available from ultra-high-resolution structures of proteins as an alternative to neutron diffraction and other methods such as NMR structural analysis.
    Nature 01/2015; DOI:10.1038/nature14110 · 42.35 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Hydrogenases are enzymes that catalyze the oxidation of H2 as well as the reduction of protons to form H2. The active site of [FeFe] hydrogenase is referred to as the "H-cluster" and consists of a "classical" [4Fe-4S] cluster connected via a bridging cysteine thiol group to a unique [2Fe]H sub-cluster, containing CN(-) and CO ligands as well as a bidentate azadithiolate ligand. It has been recently shown that the biomimetic [Fe2(adt)(CO)4(CN)2](2-) (adt(2-) = azadithiolate) complex resembling the diiron sub-cluster can be inserted in vitro into the apo-protein of [FeFe] hydrogenase, which contains only the [4Fe-4S] part of the H-cluster, resulting in a fully active enzyme. This synthetic tool allows convenient incorporation of a variety of diiron mimics, thus generating hydrogenases with artificial active sites. [FeFe] hydrogenase from Chlamydomonas reinhardtii maturated with the biomimetic complex [Fe2(pdt)(CO)4(CN)2](2-) (pdt(2-) = propanedithiolate), in which the bridging adt(2-) ligand is replaced by pdt(2-), can be stabilized in a state strongly resembling the active oxidized (Hox) state of the native protein. This state is EPR active and the signal originates from the mixed valence Fe(I)Fe(II) state of the diiron sub-cluster. Taking advantage of the variant with (15)N and (13)C isotope labeled CN(-) ligands we performed HYSCORE and ENDOR studies on this hybrid protein. The (13)C hyperfine couplings originating from both CN(-) ligands were determined and assigned. Only the (15)N coupling from the CN(-) ligand bound to the terminal iron was observed. Detailed orientation selective ENDOR and HYSCORE experiments at multiple field positions enabled the extraction of accurate data for the relative orientations of the nitrogen and carbon hyperfine tensors. These data are consistent with the crystal structure assuming a g-tensor orientation following the local symmetry of the binuclear sub-cluster.
    Physical Chemistry Chemical Physics 01/2015; 17(7). DOI:10.1039/c4cp05426a · 4.20 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: A central question in biological water splitting concerns the oxidation states of the manganese ions that comprise the oxygen-evolving complex of photosystem II. Understanding the nature and order of oxidation events that occur during the catalytic cycle of five Si states (i = 0–4) is of fundamental importance both for the natural system and for artificial water oxidation catalysts. Despite the widespread adoption of the so-called “high-valent scheme”—where, for example, the Mn oxidation states in the S2 state are assigned as III, IV, IV, IV—the competing “low-valent scheme” that differs by a total of two metal unpaired electrons (i.e. III, III, III, IV in the S2 state) is favored by several recent studies for the biological catalyst. The question of the correct oxidation state assignment is addressed here by a detailed computational comparison of the two schemes using a common structural platform and theoretical approach. Models based on crystallographic constraints were constructed for all conceivable oxidation state assignments in the four (semi)stable S states of the oxygen evolving complex, sampling various protonation levels and patterns to ensure comprehensive coverage. The models are evaluated with respect to their geometric, energetic, electronic, and spectroscopic properties against available experimental EXAFS, XFEL-XRD, EPR, ENDOR and Mn K pre-edge XANES data. New 2.5 K 55Mn ENDOR data of the S2 state are also reported. Our results conclusively show that the entire S state phenomenology can only be accommodated within the high-valent scheme by adopting a single motif and protonation pattern that progresses smoothly from S0 (III, III, III, IV) to S3 (IV, IV, IV, IV), satisfying all experimental constraints and reproducing all observables. By contrast, it was impossible to construct a consistent cycle based on the low-valent scheme for all S states. Instead, the low-valent models developed here may provide new insight into the over-reduced S states and the states involved in the assembly of the catalytically active water oxidizing cluster.
    Chemical Science 01/2015; 6(3). DOI:10.1039/C4SC03720K · 8.60 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The structural and dynamical interaction of proteins with their microenvironment in disordered matrices plays a decisive role for their function; EPR spectroscopy is a powerful tool for shading light onto the molecular mechanisms of this protein–matrix interplay. To clarify the molecular mechanisms of disaccharide bioprotection, we studied the structure and dynamics of spin-labeled systems and photosynthetic reaction centers (RCs) in sucrose and trehalose matrices at different hydration levels by means of cw and pulse high-field 95 GHz (W-band) EPR as well as by FTIR. In this minireview, we summarize and discuss EPR and FTIR experiments showing that the anhydrobiotic state of the RC–trehalose system (1) is not the result of matrix-induced changes of the local structure of the charge-separated radical-pair cofactors, \({\text{P}}_{865}^{ \cdot + }\) and \({\text{Q}}_{\text{A}}^{ \cdot - }\) , and (2) is not the result of changes of local dynamics and local hydrogen bonding of QA in its binding pocket. Rather, the extreme impairment of RC dynamics caused by incorporation into the dehydrated trehalose matrix, which also protects it against thermal denaturation, originates in the high rigidity, already at room temperature, of the dry trehalose glass matrix coating the RC protein surface. This surface hydrogen-bonding scaffold shifts the correlation time of thermal conformational fluctuations into the non-biological time domain. Another intriguing aspect of disaccharide bioprotection is the superior efficiency of trehalose versus sucrose matrices in stabilizing the anhydrobiotic state of proteins. To clarify the molecular basis of this specificity, glassy trehalose–water and sucrose–water binary systems, incorporating a nitroxide radical as spin probe, have been studied by high-field W-band EPR spectroscopy at different water contents. Analysis of the EPR spectra revealed a different structural and dynamical organization in the sucrose and trehalose matrix, only the trehalose being homogeneous in terms of residual water and nitroxide distribution.
    Applied Magnetic Resonance 01/2015; DOI:10.1007/s00723-014-0633-4 · 1.15 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The influence of β-lactoglobulin (βLG) on the fast sub-picosecond collective hydration dynamics in the solvent was investigated by THz absorption spectroscopy as a function of pH. It is well-known that a change in pH from pH 6 to pH 8 reversibly opens or closes the binding cavity by a transition of the E-F loop. Furthermore, the aggregation of the protein into dimers is affected, which is thought to be triggered by changes in the enzyme's electrostatic potential. Our data reveal that pH has a clear influence on the THz absorption of βLG. We discuss this influence in light of the changes observed in the sub-psec solute/solvent dynamics when probed by THz spectroscopy, which are, in turn, seen to correlate with changes in the pH value.
    The Journal of Chemical Physics 12/2014; 141(22):22D534. DOI:10.1063/1.4903237 · 3.12 Impact Factor
  • Hideaki Ogata, Wolfgang Lubitz
    [Show abstract] [Hide abstract]
    ABSTRACT: A new perspective on enzymes: Free-electron lasers are increasingly used to obtain crystal structures of interesting enzymes like photosystem II from nanocrystals at room temperature, to avoid radiation damage, and to detect structural differences between specific states in the catalytic cycle.
    Angewandte Chemie International Edition in English 11/2014; 53(48). DOI:10.1002/anie.201408672 · 13.45 Impact Factor
  • Hideaki Ogata, Wolfgang Lubitz
    Angewandte Chemie 11/2014; 126(48). DOI:10.1002/ange.201408672
  • [Show abstract] [Hide abstract]
    ABSTRACT: Bacteriochlorophyll a biosynthesis requires the stereo- and regiospecific two electron reduction of the C7-C8 double bond of chlorophyllide a by the nitrogenase-like multisubunit metalloenzyme, chlorophyllide a oxidoreductase (COR). ATP-dependent COR catalysis requires interaction of protein subcomplex (BchX)2 with the catalytic (BchY/BchZ)2 protein to facilitate substrate reduction via two redox active iron-sulfur centers. The ternary COR enzyme holocomplex comprising subunits BchX, BchY, and BchZ from the purple bacterium Roseobacter denitrificans was trapped in the presence of the ATP transition state analog ADP-AlF4 (-). Electron paramagnetic resonance experiments revealed a [4Fe-4S] cluster of subcomplex (BchX)2. A second [4Fe-4S] cluster was identified on (BchY/BchZ)2. Mutagenesis experiments indicated that the latter is ligated by four cysteines which is in contrast to the three cysteine/one aspartate ligation pattern of the closely related dark-operative protochlorophyllide a oxidoreductase (DPOR). In subsequent mutagenesis experiments a DPOR-like aspartate ligation pattern was implemented for the catalytic [4Fe-4S] cluster of COR. Artificial cluster formation for this inactive COR variant was demonstrated spectroscopically. A series of chemically modified substrate molecules with altered substituents on the individual pyrrole rings and the isocyclic ring were tested as COR substrates. The COR enzyme was still able to reduce the B ring of substrates carrying modified substituents on ring systems A, C, and E. However, substrates with a modification of the distantly located propionate side chain were not accepted. A tentative substrate binding mode was concluded in analogy to the related DPOR system. Copyright © 2014, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 11/2014; 290(2). DOI:10.1074/jbc.M114.617761 · 4.60 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Based on the widely applied fluorogenic peptide FS-6 (Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2; Mca = methoxycoumarin-4-acetyl; Dpa = N-3-(2,4-dinitrophenyl)l-α,β-diaminopropionyl) a caged substrate peptide Ac-Lys-Pro-Leu-Gly-Lys*-Lys-Ala-Arg-NH2 (*, position of the cage group) for matrix metalloproteinases was synthesized and characterized. The synthesis implies the modification of a carbamidated lysine side-chain amine with a photocleavable 2-nitrobenzyl group. Mass spectrometry upon UV irradiation demonstrated the complete photolytic cleavage of the protecting group. Time-resolved laser-flash photolysis at 355 nm in combination with transient absorption spectroscopy determined the biphasic decomposition with τa = 171 ± 3 ms (79%) and τb = 2.9 ± 0.2 ms (21%) at pH 6.0 of the photo induced release of 2-nitrobenzyl group. The recombinantly expressed catalytic domain of human membrane type I matrix metalloproteinase (MT1-MMP or MMP-14) was used to determine the hydrolysis efficiency for the caged peptide before and after photolysis. It turned out that the cage group sufficiently shields the peptide from peptidase activity, which can be thus controlled by UV light.
    Photochemical and Photobiological Sciences 11/2014; 14(2). DOI:10.1039/C4PP00297K · 2.92 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Hydrogenases are nature's efficient catalysts for both the generation of energy via oxidation of molecular hydrogen and the production of hydrogen via the reduction of protons. However, their O2 sensitivity and deactivation at high potential limit their applications in practical devices, such as fuel cells. Here, we show that the integration of an O2-sensitive hydrogenase into a specifically designed viologen-based redox polymer protects the enzyme from O2 damage and high-potential deactivation. Electron transfer between the polymer-bound viologen moieties controls the potential applied to the active site of the hydrogenase and thus insulates the enzyme from excessive oxidative stress. Under catalytic turnover, electrons provided from the hydrogen oxidation reaction induce viologen-catalysed O2 reduction at the polymer surface, thus providing self-activated protection from O2. The advantages of this tandem protection are demonstrated using a single-compartment biofuel cell based on an O2-sensitive hydrogenase and H2/O2 mixed feed under anode-limiting conditions.
    Nature Chemistry 09/2014; 6(9):822-7. DOI:10.1038/nchem.2022 · 21.76 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The electronic structure of the Mn/Fe cofactor identified in a new class of oxidases (R2lox) described by Andersson and Högbom [Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 5633] is reported. The R2lox protein is homologous to the small subunit of class Ic ribonucleotide reductase (R2c), but has a completely different in vivo function. Using multifrequency EPR and related pulse techniques, it is shown that the cofactor of R2lox represents an antiferromagnetically coupled Mn(III)/Fe(III) dimer linked by a μ-hydroxo/bis-μ-carboxylato bridging network. The Mn(III) ion is coordinated by a single water ligand. The R2lox cofactor is photoactive, converting into a second form (R2loxPhoto) upon visible illumination at cryogenic temperatures (77 K) that completely decays upon warming. This second, unstable form of the cofactor more closely resembles the Mn(III)/Fe(III) cofactor seen in R2c. It is shown that the two forms of the R2lox cofactor differ primarily in terms of the local site geometry and electronic state of the Mn(III) ion, as best evidenced by a reorientation of its unique (55)Mn hyperfine axis. Analysis of the metal hyperfine tensors in combination with density functional theory (DFT) calculations suggest that this change is triggered by deprotonation of the μ-hydroxo bridge. These results have important consequences for mixed-metal R2c cofactor and the divergent chemistry these two systems perform.
    Journal of the American Chemical Society 08/2014; 136(38). DOI:10.1021/ja507435t · 11.44 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The photosynthetic protein complex photosystem II oxidizes water to molecular oxygen at an embedded tetramanganese-calcium cluster. Resolving the geometric and electronic structure of this cluster in its highest metastable catalytic state (designated S3) is a prerequisite for understanding the mechanism of O-O bond formation. Here, multifrequency, multidimensional magnetic resonance spectroscopy reveals that all four manganese ions of the catalyst are structurally and electronically similar immediately before the final oxygen evolution step; they all exhibit a 4+ formal oxidation state and octahedral local geometry. Only one structural model derived from quantum chemical modeling is consistent with all magnetic resonance data; its formation requires the binding of an additional water molecule. O-O bond formation would then proceed by the coupling of two proximal manganese-bound oxygens in the transition state of the cofactor.
    Science 08/2014; 345(6198):804-8. DOI:10.1126/science.1254910 · 31.48 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Photohydrogen generation in microalgae is catalysed by hydroge-nases, which receive electrons from photosystem I via the ferredoxin PETF. The dominant acceptor of photosynthetic electrons is, however, ferredoxin-NADP + -oxidoreductase (FNR). By utilizing targeted ferre-doxin and FNR variants in a light-dependent competition assay, electrons can be redirected to the hydrogenase yielding a five-fold enhanced hydrogen evolution activity.
    Energy & Environmental Science 07/2014; 7(10). DOI:10.1039/c4ee01444h · 15.49 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Please find the abstract attached as a separate word file "abstract".
    Journal of the American Chemical Society 07/2014; 136(32). DOI:10.1021/ja503390c · 11.44 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: A series of four [S2Ni(μ-S)2FeCp*Cl] compounds with different tetradentate thiolate/thioether ligands bound to the Ni(II) ion is reported (Cp* = C5Me5). The {S2Ni(μ-S)2Fe} core of these compounds resembles structural features of the active site of [NiFe] hydrogenases. Detailed analyses of the electronic structures of these compounds by Mössbauer and electron paramagnetic resonance spectroscopy, magnetic measurements, and density functional theory calculations reveal the oxidation states Ni(II) low spin and Fe(II) high spin for the metal ions. The same electronic configurations have been suggested for the Cred1 state of the C-cluster [NiFeu] subsite in carbon monoxide dehydrogenases (CODH). The Ni-Fe distance of ∼3 Å excludes a metal-metal bond between nickel and iron, which is in agreement with the computational results. Electrochemical experiments show that iron is the redox active site in these complexes, performing a reversible one-electron oxidation. The four complexes are discussed with regard to their similarities and differences both to the [NiFe] hydrogenases and the C-cluster of Ni-containing CODH.
    Inorganic Chemistry 06/2014; 53(12). DOI:10.1021/ic500910z · 4.79 Impact Factor
  • Johannes Messinger, Wolfgang Lubitz, Jian-Ren Shen
    Physical Chemistry Chemical Physics 05/2014; 16(24). DOI:10.1039/c4cp90053g · 4.20 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Base metal, molecular catalysts for the fundamental process of conversion of protons and electrons to dihydrogen, remain a substantial synthetic goal related to a sustainable energy future. Here we report a diiron complex with bridging thiolates in the butterfly shape of the 2Fe2S core of the [FeFe]-hydrogenase active site but with nitrosyl rather than carbonyl or cyanide ligands. This binuclear [(NO)Fe(N2S2)Fe(NO)2](+) complex maintains structural integrity in two redox levels; it consists of a (N2S2)Fe(NO) complex (N2S2=N,N'-bis(2-mercaptoethyl)-1,4-diazacycloheptane) that serves as redox active metallodithiolato bidentate ligand to a redox active dinitrosyl iron unit, Fe(NO)2. Experimental and theoretical methods demonstrate the accommodation of redox levels in both components of the complex, each involving electronically versatile nitrosyl ligands. An interplay of orbital mixing between the Fe(NO) and Fe(NO)2 sites and within the iron nitrosyl bonds in each moiety is revealed, accounting for the interactions that facilitate electron uptake, storage and proton reduction.
    Nature Communications 05/2014; 5:3684. DOI:10.1038/ncomms4684 · 10.74 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The EPR "split signals" represent key intermediates of the S-state cycle where the redox active D1-Tyr161 (YZ) has been oxidized by the reaction center of the photosystem II enzyme to its tyrosyl radical form, but the successive oxidation of the Mn4CaO5 cluster has not yet occurred (SiYZ˙). Here we focus on the S2YZ˙ state, which is formed en route to the final metastable state of the catalyst, the S3 state, the state which immediately precedes O-O bond formation. Quantum chemical calculations demonstrate that both isomeric forms of the S2 state, the open and closed cubane isomers, can form states with an oxidized YZ˙ residue without prior deprotonation of the Mn4CaO5 cluster. The two forms are expected to lie close in energy and retain the electronic structure and magnetic topology of the corresponding S2 state of the inorganic core. As expected, tyrosine oxidation results in a proton shift towards His190. Analysis of the electronic rearrangements that occur upon formation of the tyrosyl radical suggests that a likely next step in the catalytic cycle is the deprotonation of a terminal water ligand (W1) of the Mn4CaO5 cluster. Diamagnetic metal ion substitution is used in our calculations to obtain the molecular g-tensor of YZ˙. It is known that the gx value is a sensitive probe not only of the extent of the proton shift between the tyrosine-histidine pair, but also of the polarization environment of the tyrosine, especially about the phenolic oxygen. It is shown for PSII that this environment is determined by the Ca(2+) ion, which locates two water molecules about the phenoxyl oxygen, indirectly modulating the oxidation potential of YZ.
    Physical Chemistry Chemical Physics 04/2014; 16(24). DOI:10.1039/c4cp00696h · 4.20 Impact Factor

Publication Stats

8k Citations
1,905.71 Total Impact Points

Institutions

  • 2006–2015
    • Max Planck Institute for Chemical Energy Conversion
      Mülheim-on-Ruhr, North Rhine-Westphalia, Germany
  • 2003–2013
    • Max Planck Institute for Chemistry
      Mayence, Rheinland-Pfalz, Germany
    • Humboldt-Universität zu Berlin
      Berlín, Berlin, Germany
  • 1991–2010
    • Technische Universität Berlin
      • Department of Chemistry
      Berlín, Berlin, Germany
  • 2009
    • University of Bonn
      • Institute of Physical and Theoretical Chemistry
      Bonn, North Rhine-Westphalia, Germany
  • 2007
    • Semenov Institute of Chemical Physics
      Moskva, Moscow, Russia
  • 1999–2007
    • University of Amsterdam
      Amsterdamo, North Holland, Netherlands
  • 2005
    • John Innes Centre
      • Department of Biological Chemistry
      Norwich, ENG, United Kingdom
  • 1975–2003
    • Freie Universität Berlin
      • Institute of Experimental Physics
      Berlín, Berlin, Germany
  • 1996–2001
    • Stockholm University
      Tukholma, Stockholm, Sweden
  • 2000
    • Uppsala University
      Uppsala, Uppsala, Sweden
  • 1996–1998
    • Arizona State University
      • Department of Chemistry and Biochemistry
      Phoenix, Arizona, United States
  • 1995
    • Max Planck Institute for Biophysical Chemistry
      Göttingen, Lower Saxony, Germany
  • 1984–1995
    • University of California, San Diego
      • Department of Physics
      San Diego, California, United States