TY  - JOUR
AB  - The engineered lipocalin Colchicalin binds the clinically relevant plant toxin colchicine with picomolar affinity. X-ray structures revealed major loop rearrangements at the open end of the β-barrel upon ligand binding, suggesting a critical role for protein dynamics. Here, we integrated solution NMR relaxation experiments with molecular dynamics (MD) simulations and Markov modelling to examine conformational dynamics in the free and ligand-bound Colchicalin on the picosecond-to-millisecond timescale. Fast backbone dynamics were comparable in the presence and absence of colchicine, indicating preserved secondary structure. However, large-scale fluctuations in the structurally variable loops on the microsecond-to-millisecond timescale were observed in the apo form. We identified conformational exchange between three states, binding competent, partially closed and fully closed, characterised by loop L3 rearrangements. Colchicine binding quenches these motions, indicating a strong interplay between protein dynamics and ligand recognition. Our results support conformational selection over induced fit as the binding mechanism, highlighting the critical role of slow-timescale dynamics to enable specific, high-affinity ligand recognition and providing an important example for rational drug design.
AU  - Bostock, M.J.
AU  - Kolloff, C.*
AU  - Jerschke, E.*
AU  - Asami, S.*
AU  - Skerra, A.*
AU  - Olsson, S.*
AU  - Sattler, M.
C1  - 75865
C2  - 58163
TI  - Conformational quenching in an engineered lipocalin protein achieves high affinity binding to the toxin colchicine.
JO  - Angew. Chem.-Int. Edit.
PY  - 2025
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Amyloid self-assembly of α-synuclein (αSyn) is linked to the pathogenesis of Parkinson's disease (PD). Type 2 diabetes (T2D) has recently emerged as a risk factor for PD. Cross-interactions between their amyloidogenic proteins may act as molecular links. In fact, fibrils of islet amyloid polypeptide (IAPP) (T2D) can cross-seed αSyn amyloidogenesis and αSyn and IAPP colocalize in PD brains. Inhibition of both self- and IAPP-cross-seeded αSyn amyloidogenesis could thus interfere with PD pathogenesis. Here we show that macrocyclic peptides, designed to mimic IAPP self-/cross-interaction sites and previously found to inhibit amyloidogenesis of IAPP and/or Alzheimer's disease (AD) amyloid-β peptide Aβ40(42), are nanomolar inhibitors of both self- and IAPP-cross-seeded amyloid self-assembly of αSyn. Anti-amyloid function is mediated by nanomolar affinity interactions with αSyn via three αSyn regions which are identified as key sites of both αSyn self-assembly and its cross-interactions with IAPP. We also show that the peptides block Aβ42-mediated cross-seeding of αSyn as well. Based on their broad spectrum anti-amyloid function and additional drug-like features, these peptides are leads for multifunctional anti-amyloid drugs in PD, T2D, AD, and their comorbidities, while the identified αSyn key segments are valuable targets for novel, multi-site targeting amyloid inhibitors in PD and related synucleinopathies.
AU  - Hornung, S.*
AU  - Vogl, D.P.*
AU  - Naltsas, D.*
AU  - Dalla Volta, B.*
AU  - Ballmann, M.*
AU  - Marcon, B.*
AU  - Syed, M.M.K.*
AU  - Wu, Y.*
AU  - Spanopoulou, A.*
AU  - Feederle, R.
AU  - Heidrich, L.*
AU  - Bernhagen, J.*
AU  - Koeglsperger, T.*
AU  - Höglinger, G.U.*
AU  - Rammes, G.*
AU  - Lashuel, H.A.*
AU  - Kapurniotu, A.*
C1  - 73091
C2  - 56909
CY  - Postfach 101161, 69451 Weinheim, Germany
TI  - Multi-targeting macrocyclic peptides as nanomolar inhibitors of self- and cross-seeded amyloid self-assembly of α-synuclein.
JO  - Angew. Chem.-Int. Edit.
PB  - Wiley-v C H Verlag Gmbh
PY  - 2025
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Optoacoustic (or photoacoustic) imaging promises micron-resolution noninvasive bioimaging with much deeper penetration (>cm) than fluorescence. However, optoacoustic imaging of enzyme activity would require loud, photostable, NIR-absorbing molecular contrast agents: which remain unknown. Most organic molecular contrast agents are repurposed fluorophores, with severe shortcomings of photoinstability or phototoxicity under optoacoustic imaging, as consequences of their slow S1→S0 electronic relaxation. We now report that known fluorophores can be rationally modified to reach ultrafast S1→S0 rates, without much extra molecular complexity, simply by merging them with molecular switches. Here, we merge azobenzene switches to cyanine dyes to give ultrafast relaxation (<10 ps, >100-fold faster). Without even adapting instrument settings, these azohemicyanines display outstanding improvements in signal longevity (>1000-fold increase of photostability) and signal loudness (here: >3-fold even at time zero). We show why this simple but unexplored design strategy can still offer stronger performance in the future, and can also increase the spatial resolution and the quantitative linearity of photoacoustic response over extended longitudinal imaging. By bringing the world of molecular switches and rotors to bear on problems facing optoacoustic agents, this practical strategy will help to unleash the full potential of optoacoustic imaging in fundamental studies and translational uses.
AU  - Müller, M.*
AU  - Liu, N.
AU  - Gujrati, V.
AU  - Valavalkar, A.*
AU  - Hartmann, S.*
AU  - Anzenhofer,P.
AU  - Klemm, U.
AU  - Telek, A.*
AU  - Dietzek-Ivanšić, B.*
AU  - Hartschuh, A.*
AU  - Ntziachristos, V.
AU  - Thorn-Seshold, O.*
C1  - 70775
C2  - 55743
CY  - Postfach 101161, 69451 Weinheim, Germany
TI  - Merged molecular switches excel as optoacoustic dyes: Azobenzene-cyanines are loud and photostable NIR imaging agents.
JO  - Angew. Chem.-Int. Edit.
PB  - Wiley-v C H Verlag Gmbh
PY  - 2024
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Protein homeostasis in bacteria is regulated by proteases such as the tetradecameric caseinolytic protease P (ClpP). Although substrates of ClpP have been successfully deciphered in genetically engineered cells, methods which directly trap processed proteins within native cells remain elusive. Here, we introduce an in situ trapping strategy which utilizes trifunctional probes that bind to the active site serine of ClpP and capture adjacent substrates with an attached photocrosslinking moiety. After enrichment using an alkyne handle, substrate deconvolution by mass spectrometry (MS) is performed. We show that our two traps bind substoichiometrically to ClpP, retain protease activity, exhibit unprecedented selectivity for Staphylococcus aureus ClpP in living cells and capture numerous known and novel substrates. The exemplary validation of trapped hits using a targeted proteomics approach confirmed the fidelity of this technology. In conclusion, we provide a novel chemical platform suited for the discovery of serine protease substrates beyond genetic engineering.
AU  - Sieber, S.A.*
AU  - Gronauer, T.F.
AU  - Eck, L.K.*
AU  - Ludwig, C.*
C1  - 71377
C2  - 56083
CY  - Postfach 101161, 69451 Weinheim, Germany
TI  - A photocrosslinking probe to capture the substrates of caseinolytic protease P.
JO  - Angew. Chem.-Int. Edit.
PB  - Wiley-v C H Verlag Gmbh
PY  - 2024
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Designed peptides derived from the islet amyloid polypeptide (IAPP) cross-amyloid interaction surface with A beta (termed interaction surface mimics or ISMs) have been shown to be highly potent inhibitors of A beta amyloid self-assembly. However, the molecular mechanism of their function is not well understood. Using solution-state and solid-state NMR spectroscopy in combination with ensemble-averaged dynamics simulations and other biophysical methods including TEM, fluorescence spectroscopy and microscopy, and DLS, we characterize ISM structural preferences and interactions. We find that the ISM peptide R3-GI is highly dynamic, can adopt a beta-like structure, and oligomerizes into colloid-like assemblies in a process that is reminiscent of liquid-liquid phase separation (LLPS). Our results suggest that such assemblies yield multivalent surfaces for interactions with A beta 40. Sequestration of substrates into these colloid-like structures provides a mechanistic basis for ISM function and the design of novel potent anti-amyloid molecules.
AU  - Niu, Z.
AU  - Prade, E.*
AU  - Malideli, E.*
AU  - Hille, K.*
AU  - Jussupow, A.*
AU  - Mideksa, Y.G.*
AU  - Yan, L.M.*
AU  - Qian, C.*
AU  - Fleisch, M.
AU  - Messias, A.C.
AU  - Sarkar, R.
AU  - Sattler, M.
AU  - Lamb, D.C.*
AU  - Feige, M.J.*
AU  - Camilloni, C.*
AU  - Kapurniotu, A.*
AU  - Reif, B.
C1  - 58015
C2  - 48023
CY  - Postfach 101161, 69451 Weinheim, Germany
SP  - 2-13
TI  - Structural insight into IAPP-derived amyloid inhibitors and their mechanism of action.
JO  - Angew. Chem.-Int. Edit.
VL  - 59
IS  - 14
PB  - Wiley-v C H Verlag Gmbh
PY  - 2020
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - The large-scale and label-free molecular characterization of single cells in their natural tissue habitat remains a major challenge in molecular biology. We present a method that integrates morphometric image analysis to delineate and classify individual cells with their single-cell-specific molecular profiles. This approach provides a new means to study spatial biological processes such as cancer field effects and the relationship between morphometric and molecular features.
AU  - Ščupáková, K.*
AU  - Dewez, F.*
AU  - Walch, A.K.
AU  - Heeren, R.M.A.*
AU  - Balluff, B.*
C1  - 59949
C2  - 48951
CY  - Postfach 101161, 69451 Weinheim, Germany
SP  - 17600-17603
TI  - Morphometric cell classification for single-Cell MALDI-mass spectrometry imaging.
JO  - Angew. Chem.-Int. Edit.
VL  - 132
IS  - 40
PB  - Wiley-v C H Verlag Gmbh
PY  - 2020
SN  - 1433-7851
ER  - 

TY  - JOUR
AU  - Jagtap, P.K.A.*
AU  - Asami, S.*
AU  - Sippel, C.*
AU  - Kaila, V.R.I.*
AU  - Hausch, F.*
AU  - Sattler, M.
C1  - 56849
C2  - 47258
CY  - Postfach 101161, 69451 Weinheim, Germany
TI  - Selective inhibitors of FKBP51 employ conformational selection of dynamic invisible states (vol 58, pg 9429, 2019).
JO  - Angew. Chem.-Int. Edit.
PB  - Wiley-v C H Verlag Gmbh
PY  - 2019
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - The recently discovered SAFit class of inhibitors against the Hsp90 co-chaperone FKBP51 show greater than 10 000-fold selectivity over its closely related paralogue FKBP52. However, the mechanism underlying this selectivity remained unknown. By combining NMR spectroscopy, biophysical and computational methods with mutational analysis, we show that the SAFit molecules bind to a transient pocket in FKBP51. This represents a weakly populated conformation resembling the inhibitor-bound state of FKBP51, suggesting conformational selection rather than induced fit as the major binding mechanism. The inhibitor-bound conformation of FKBP51 is stabilized by an allosteric network of residues located away from the inhibitor-binding site. These residues stabilize the Phe67 side chain in a dynamic outward conformation and are distinct in FKBP52, thus rationalizing the basis for the selectivity of SAFit inhibitors. Our results represent a paradigm for the selective inhibition of transient binding pockets.
AU  - Jagtap, P.K.A.*
AU  - Asami, S.*
AU  - Sippel, C.*
AU  - Kaila, V.R.I.*
AU  - Hausch, F.*
AU  - Sattler, M.
C1  - 56908
C2  - 47259
SP  - 9429-9433
TI  - Selective inhibitors of FKBP51 employ conformational selection of dynamic invisible states.
JO  - Angew. Chem.-Int. Edit.
VL  - 58
IS  - 28
PY  - 2019
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Novel targets are needed for treatment of devastating diseases such as cancer. For decades, natural products have guided innovative therapies by addressing diverse pathways. Inspired by the potent cytotoxic bioactivity of myxobacterial vioprolides A-D, we performed in-depth studies on their mode of action. Based on its prominent potency against human acute lymphoblastic leukemia (ALL) cells, we conducted thermal proteome profiling (TPP) and deciphered the target proteins of the most active derivative vioprolide A (VioA) in Jurkat cells. Nucleolar protein 14 (NOP14), which is essential in ribosome biogenesis, was confirmed as a specific target of VioA by a suite of proteomic and biological follow-up experiments. Given its activity against ALL cells compared to healthy lymphocytes, VioA exhibits unique therapeutic potential for anticancer therapy through a novel mode of action.
AU  - Kirsch, V.C.*
AU  - Orgler, C.*
AU  - Braig, S.*
AU  - Jeremias, I.
AU  - Auerbach, D.*
AU  - Müller, R.*
AU  - Vollmar, A.M.*
AU  - Sieber, S.A.*
C1  - 57679
C2  - 47874
CY  - Postfach 101161, 69451 Weinheim, Germany
SP  - 1595-1600
TI  - The cytotoxic natural product vioprolide A targets nucleolar protein 14 essential for ribosome biogenesis.
JO  - Angew. Chem.-Int. Edit.
VL  - 59
IS  - 4
PB  - Wiley-v C H Verlag Gmbh
PY  - 2019
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Magic-angle spinning (MAS) is an essential ingredient in a wide variety of solid-state NMR experiments. The standard procedures to adjust the rotor angle are not highly accurate, resulting in a slight misadjustment of the rotor from the magic angle (RL= ) on the order of a few millidegrees. This small missetting has no significant impact on the overall spectral resolution, but is sufficient to reintroduce anisotropic interactions. Shown here is that site-specific H-1-N-15 dipolar couplings can be accurately measured in a heavily deuterated protein. This method can be applied at arbitrarily high MAS frequencies, since neither rotor synchronization nor particularly high radiofrequency field strengths are required. The off-MAS method allows the quantification of order parameters for very dynamic residues, which often escape an analysis using existing methods.
AU  - Xue, K.
AU  - Mühlbauer, M.
AU  - Mamone, S.*
AU  - Sarkar, R.
AU  - Reif, B.
C1  - 55356
C2  - 46340
CY  - Postfach 101161, 69451 Weinheim, Germany
SP  - 4286-4290
TI  - Accurate determination of H-1-N-15 dipolar couplings using inaccurate settings of the magic angle in solid-state NMR spectroscopy.
JO  - Angew. Chem.-Int. Edit.
VL  - 58
IS  - 13
PB  - Wiley-v C H Verlag Gmbh
PY  - 2019
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - NMR spectroscopy at ultra-high magnetic fields requires improved radiofrequency (rf) pulses to cover the increased spectral bandwidth. Optimized 90 degrees pulse pairs were introduced as Ramsey-type cooperative (Ram-COOP) pulses for biomolecular NMR applications. The Ram-COOP element provides broadband excitation with enhanced sensitivity and reduced artifacts even at magnetic fields >1.0GHz H-1 Larmor frequency (23T). A pair of 30s Ram-COOP pulses achieves an excitation bandwidth of 100kHz with a maximum rf field of 20kHz, more than three-fold improved compared to excitation by rectangular pulses. Ram-COOP pulses exhibit little offset-dependent phase errors and are robust to rf inhomogeneity. The performance of the Ram-COOP element is experimentally confirmed with heteronuclear multidimensional NMR experiments, applied to proteins and nucleic acids. Ram-COOP provides broadband excitation at low rf field strength suitable for application at current magnetic fields and beyond 23T.
AU  - Asami, S.*
AU  - Kallies, W.*
AU  - Guenther, J.C.*
AU  - Stavropoulou, M.*
AU  - Glaser, S.J.*
AU  - Sattler, M.
C1  - 54692
C2  - 45769
CY  - Postfach 101161, 69451 Weinheim, Germany
SP  - 14498-14502
TI  - Ultrashort broadband cooperative pulses for multidimensional bio-molecular NMR experiments.
JO  - Angew. Chem.-Int. Edit.
VL  - 57
IS  - 44
PB  - Wiley-v C H Verlag Gmbh
PY  - 2018
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - The total synthesis of the naturally occurring antibiotic GE81112A, a densely functionalized tetrapeptide, is reported. Comparison of spectral data with those of the natural product and the lack of biological activity of the synthesized compound led us to revise the published configuration of the 3-hydroxypipecolic acid moiety. This hypothesis was fully validated by the synthesis of the corresponding epimer.
AU  - Jürjens, G.
AU  - Schuler, S.M.M.*
AU  - Kurz, M.*
AU  - Petit, S.*
AU  - Couturier, C.*
AU  - Jeannot, F.*
AU  - Nguyen, F.*
AU  - Wende, R.C.*
AU  - Hammann, P.E.*
AU  - Wilson, D.N.*
AU  - Bacqué, E.*
AU  - Pöverlein, C.*
AU  - Bauer, A.*
C1  - 53928
C2  - 45100
CY  - Postfach 101161, 69451 Weinheim, Germany
SP  - 12157-12161
TI  - Total synthesis and structural revision of the antibiotic tetrapeptide GE81112A.
JO  - Angew. Chem.-Int. Edit.
VL  - 57
IS  - 37
PB  - Wiley-v C H Verlag Gmbh
PY  - 2018
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Tudor domains bind to dimethylarginine (DMA) residues, which are post-translational modifications that play a central role in gene regulation in eukaryotic cells. NMR spectroscopy and quantum calculations are combined to demonstrate that DMA recognition by Tudor domains involves conformational selection. The binding mechanism is confirmed by a mutation in the aromatic cage that perturbs the native recognition mode of the ligand. General mechanistic principles are delineated from the combined results, indicating that Tudor domains utilize cation–π interactions to achieve ligand recognition.
AU  - Supekar, S.*
AU  - Papageorgiou, A.C.*
AU  - Gemmecker, G.
AU  - Peltzer, R.*
AU  - Johansson, M.P.*
AU  - Tripsianes, K.*
AU  - Sattler, M.
AU  - Kaila, V.R.I.*
C1  - 52707
C2  - 44209
CY  - Weinheim
SP  - 486-490
TI  - Conformational selection of dimethylarginine recognition by the survival motor neuron tudor domain.
JO  - Angew. Chem.-Int. Edit.
VL  - 57
IS  - 2
PB  - Wiley-v C H Verlag Gmbh
PY  - 2018
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Dipolar recoupling in solid‐state NMR is an essential method for establishing correlations between nuclei that are close in space. In applications on protein samples, the traditional experiments like ramped and adiabatic DCP suffer from the fact that dipolar recoupling occurs only within a limited volume of the sample. This selection is dictated by the radiofrequency (rf) field inhomogeneity profile of the excitation solenoidal coil. We employ optimal control strategies to design dipolar recoupling sequences with substantially larger responsive volume and increased sensitivity. We show that it is essential to compensate for additional temporal modulations induced by sample rotation in a spatially inhomogeneous rf field. Such modulations interfere with the pulse sequence and decrease its performance. Using large‐scale optimizations we developed pulse schemes for magnetization transfer from amide nitrogen to carbonyl (NCO) as well as aliphatic carbons (NCA). Our experiments yield a signal intensity increased by a factor of 1.5 and 2.0 for NCA and NCO transfers, respectively, compared to conventional ramped DCP sequences. Consistent results were obtained using several biological samples and NMR instruments.
AU  - Tošner, Z.*
AU  - Sarkar, R.
AU  - Becker-Baldus, J.*
AU  - Glaubitz, C.*
AU  - Wegner, S.*
AU  - Engelke, F.*
AU  - Glaser, S.J.*
AU  - Reif, B.
C1  - 54572
C2  - 45667
SP  - 14722-14726
TI  - Overcoming volume selectivity of dipolar recoupling in biological solid-state NMR spectroscopy
JO  - Angew. Chem.-Int. Edit.
VL  - 130
PY  - 2018
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Covalently binding molecules are frequently regarded as being generally promiscuous. In a recent study, binding selectivities and cellular target proteins of a wide variety of reactive fragments are examined in a proteome-wide context.
AU  - Plettenburg, O.
C1  - 50224
C2  - 42241
CY  - Weinheim
SP  - 446-448
TI  - What do reactive fragments actually do in cells?
JO  - Angew. Chem.-Int. Edit.
VL  - 56
IS  - 2
PB  - Wiley-v C H Verlag Gmbh
PY  - 2017
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Multi-domain proteins play critical roles in fine-tuning essential processes in cellular signaling and gene regulation. Typically, multiple globular domains that are connected by flexible linkers undergo dynamic rearrangements upon binding to protein, DNA or RNA ligands. RNA binding proteins (RBPs) represent an important class of multi-domain proteins, which regulate gene expression by recognizing linear or structured RNA sequence motifs. Here, we employ segmental perdeuteration of the three RNA recognition motif (RRM) domains in the RBP TIA-1 using SortaseA mediated protein ligation. We show that domain-selective perdeuteration combined with contrast-matched small-angle neutron scattering (SANS), SAXS and computational modeling provides valuable information to precisely define relative domain arrangements. The approach is generally applicable to study conformational arrangements of individual domains in multi-domain proteins and changes induced by ligand binding.
AU  - Sonntag, M.
AU  - Jagtap, P.K.
AU  - Simon, B.*
AU  - Appavou, M.S.*
AU  - Geerlof, A.
AU  - Stehle, R.*
AU  - Gabel, F.*
AU  - Hennig, J.
AU  - Sattler, M.
C1  - 51538
C2  - 43293
SP  - 9322-9325
TI  - Segmental, domain-selective perdeuteration and small-angle neutron scattering for structural analysis of multi-domain proteins.
JO  - Angew. Chem.-Int. Edit.
VL  - 56
IS  - 32
PY  - 2017
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - The study of intrinsically disordered proteins (IDPs) by NMR often suffers from highly overlapped resonances that prevent unambiguous chemical-shift assignments, and data analysis that relies on well-separated resonances. We present a covalent paramagnetic lanthanide-binding tag (LBT) for increasing the chemical-shift dispersion and facilitating the chemical-shift assignment of challenging, repeat-containing IDPs. Linkage of the DOTA-based LBT to a cysteine residue induces pseudo-contact shifts (PCS) for resonances more than 20 residues from the spin-labeling site. This leads to increased chemical-shift dispersion and decreased signal overlap, thereby greatly facilitating chemical-shift assignment. This approach is applicable to IDPs of varying sizes and complexity, and is particularly helpful for repeat-containing IDPs and low-complexity regions. This results in improved efficiency for IDP analysis and binding studies.
AU  - Göbl, C.
AU  - Resch, M.
AU  - Strickland, M.*
AU  - Hartlmüller, C.
AU  - Viertler, M.
AU  - Tjandra, N.*
AU  - Madl, T.
C1  - 49796
C2  - 40937
CY  - Weinheim
SP  - 14847-14851
TI  - Increasing the chemical-shift dispersion of unstructured proteins with a covalent lanthanide shift reagent.
JO  - Angew. Chem.-Int. Edit.
VL  - 55
IS  - 47
PB  - Wiley-v C H Verlag Gmbh
PY  - 2016
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - An approach to the de novo structure prediction of proteins is described that relies on surface accessibility data from NMR paramagnetic relaxation enhancements by a soluble paramagnetic compound (sPRE). This method exploits the distance-to-surface information encoded in the sPRE data in the chemical shift-based CS-Rosetta de novo structure prediction framework to generate reliable structural models. For several proteins, it is demonstrated that surface accessibility data is an excellent measure of the correct protein fold in the early stages of the computational folding algorithm and significantly improves accuracy and convergence of the standard Rosetta structure prediction approach.
AU  - Hartlmüller, C.
AU  - Göbl, C.
AU  - Madl, T.
C1  - 49354
C2  - 41800
CY  - Weinheim
SP  - 11970-11974
TI  - Prediction of protein structure using surface accessibility data.
JO  - Angew. Chem.-Int. Edit.
VL  - 55
IS  - 39
PB  - Wiley-v C H Verlag Gmbh
PY  - 2016
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Gadolinium(III)-based contrast agents improve the sensitivity and specificity of magnetic resonance imaging (MRI), especially when targeted contrast agents are applied. Because of nonlinear correlation between the contrast agent concentration in tissue and the MRI signal obtained in vivo, quantification of certain biological or pathophysiological processes by MRI remains a challenge. Up to now, no technology has been able to provide a spatially resolved quantification of MRI agents directly within the tissue, which would allow a more precise verification of in vivo imaging results. MALDI imaging mass spectrometry for spatially resolved in situ quantification of gadolinium(III) agents, in correlation to in vivo MRI, were evaluated. Enhanced kinetics of Gadofluorine M were determined dynamically over time in a mouse model of myocardial infarction. MALDI imaging was able to corroborate the in vivo imaging MRI signals and enabled in situ quantification of the gadolinium probe with high spatial resolution.
AU  - Aichler, M.
AU  - Huber, K.
AU  - Schilling, F.*
AU  - Lohöfer, F.*
AU  - Kosanke, K.*
AU  - Meier, R.*
AU  - Rummeny, E.J.*
AU  - Walch, A.K.
AU  - Wildgruber, M.*
C1  - 43354
C2  - 36359
CY  - Weinheim
SP  - 4279-4283
TI  - Spatially resolved quantification of Gadolinium(III)-based magnetic resonance agents in tissue by MALDI imaging mass spectrometry after in vivo MRI.
JO  - Angew. Chem.-Int. Edit.
VL  - 54
IS  - 14
PB  - Wiley-v C H Verlag Gmbh
PY  - 2015
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - The design of inhibitors of protein-protein interactions mediating amyloid self-assembly is a major challenge mainly due to the dynamic nature of the involved structures and interfaces. Interactions of amyloidogenic polypeptides with other proteins are important modulators of self-assembly. Here we present a hot-segment-linking approach to design a series of mimics of the IAPP cross-amyloid interaction surface with Aβ (ISMs) as nanomolar inhibitors of amyloidogenesis and cytotoxicity of Aβ, IAPP, or both polypeptides. The nature of the linker determines ISM structure and inhibitory function including both potency and target selectivity. Importantly, ISMs effectively suppress both self- and cross-seeded IAPP self-assembly. Our results provide a novel class of highly potent peptide leads for targeting protein aggregation in Alzheimer's disease, type 2 diabetes, or both diseases and a chemical approach to inhibit amyloid self-assembly and pathogenic interactions of other proteins as well.
AU  - Andreetto, E.*
AU  - Malideli, E.*
AU  - Yan, L.M.*
AU  - Kracklauer, M.*
AU  - Farbiarz, K.*
AU  - Tatarek-Nossol, M.*
AU  - Rammes, G.*
AU  - Prade, E.
AU  - Neumüller, T.*
AU  - Caporale, A.*
AU  - Spanopoulou, A.*
AU  - Bakou, M.*
AU  - Reif, B.
AU  - Kapurniotu, A.*
C1  - 46770
C2  - 37796
SP  - 13095-13100
TI  - A hot-segment-based approach for the design of cross-amyloid interaction surface mimics as inhibitors of amyloid self-assembly.
JO  - Angew. Chem.-Int. Edit.
VL  - 54
IS  - 44
PY  - 2015
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Ultra-high-field NMR spectroscopy requires an increased bandwidth for heteronuclear decoupling, especially in biomolecular NMR applications. Composite pulse decoupling cannot provide sufficient bandwidth at practical power levels, and adiabatic pulse decoupling with sufficient bandwidth is compromised by sideband artifacts. A novel low-power, broadband heteronuclear decoupling pulse is presented that generates minimal, ultra-low sidebands. The pulse was derived using optimal control theory and represents a new generation of decoupling pulses free from the constraints of periodic and cyclic sequences. In comparison to currently available state-of-the-art methods this novel pulse provides greatly improved decoupling performance that satisfies the demands of high-field biomolecular NMR spectroscopy.
AU  - Schilling, F.*
AU  - Warner, L.R.
AU  - Gershenzon, N.I.*
AU  - Skinner, T.E.*
AU  - Sattler, M.
AU  - Glaser, S.J.*
C1  - 30913
C2  - 34010
CY  - Weinheim
SP  - 4475-4479
TI  - Next-generation heteronuclear decoupling for high-field biomolecular NMR spectroscopy.
JO  - Angew. Chem.-Int. Edit.
VL  - 53
IS  - 17
PB  - Wiley-v C H Verlag Gmbh
PY  - 2014
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - The molecular chaperone Hsp90 undergoes an ATP-driven cycle of conformational changes in which large structural rearrangements precede ATP hydrolysis. Wellestablished small-molecule inhibitors of Hsp90 compete with ATP-binding.We wondered whether compounds exist that can accelerate the conformational cycle. In a FRET-based screen reporting on conformational rearrangements in Hsp90 we identified compounds. We elucidated their mode of action and showed that they can overcome the intrinsic inhibition in Hsp90 which prevents these rearrangements. The mode of action is similar to that of the co-chaperone Aha1 which accelerates the Hsp90 ATPase. However, while the two identified compounds influence conformational changes, they target different aspects of the structural transitions. Also, the binding site determined by NMR spectroscopy is distinct. This study demonstrates that small molecules are capable of triggering specific rate-limiting transitions in Hsp90 by mechanisms similar to those in protein cofactors.
AU  - Zierer, B.K.*
AU  - Weiwad, M.*
AU  - Rübbelke, M.
AU  - Freiburger, L.
AU  - Fischer, G.S.*
AU  - Lorenz, O.R.*
AU  - Sattler, M.
AU  - Richter, K.H.*
AU  - Buchner, J.*
C1  - 42879
C2  - 35643
CY  - Weinheim
SP  - 12257-12262
TI  - Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions.
JO  - Angew. Chem.-Int. Edit.
VL  - 53
IS  - 45
PB  - Wiley-v C H Verlag Gmbh
PY  - 2014
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Both protonated and deuterated samples were employed in the study of the L7Ae box C/D RNA complex by (1) H-detected solid-state NMR spectroscopy. This approach yielded high-resolution spectra and was used to determine the intermolecular interface and extract structural parameters with high accuracy.
AU  - Asami, S.
AU  - Rakwalska-Bange, M.*
AU  - Carlomagno, T.*
AU  - Reif, B.
C1  - 23539
C2  - 31215
SP  - 2345-2349
TI  - Protein-RNA interfaces probed by 1H-detected MAS solid-state NMR spectroscopy.
JO  - Angew. Chem.-Int. Edit.
VL  - 52
IS  - 8
PB  - Wiley-VCH
PY  - 2013
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Improved Sensitivity: Efficient NMR experiments are presented for determining the secondary structure in large and dynamic RNAs using J-couplings across hydrogen bonds. The experiments provide up to eight-fold improved sensitivity and thus enable detection of base pairs in dynamic regions even in large RNAs.
AU  - Dallmann, A.
AU  - Simon, B.*
AU  - Duszczyk, M.M.
AU  - Kooshapur, H.
AU  - Pardi, A.*
AU  - Bermel, W.*
AU  - Sattler, M.
C1  - 27905
C2  - 32851
SP  - 10487-10490
TI  - Efficient detection of hydrogen bonds in dynamic regions of RNA by sensitivity-optimized NMR pulse sequences.
JO  - Angew. Chem.-Int. Edit.
VL  - 52
IS  - 40
PB  - Wiley-VCH
PY  - 2013
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Chlorhexidine and alexidine have long been used as oral disinfectants by humans. Both compounds inhibit protein-protein interactions mediated by the anti-apoptotic protein Bcl-xL at physiologically relevant concentrations and induce apoptosis in a series of tumor cell lines derived from the tongue and pharynx (see picture). Inhibition of protein-protein interactions is a potential mode of action of drugs in current human use. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
AU  - Gräber, M.*
AU  - Hell, M.*
AU  - Grost, C.*
AU  - Friberg, A.
AU  - Sperl, B.*
AU  - Sattler, M.
AU  - Berg, T.*
C1  - 24547
C2  - 31576
SP  - 4487-4491
TI  - Oral disinfectants inhibit protein-protein interactions mediated by the anti-apoptotic protein Bcl-xL and induce apoptosis in human oral tumor cells.
JO  - Angew. Chem.-Int. Edit.
VL  - 52
IS  - 16
PB  - Wiley-VCH
PY  - 2013
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Bigger is better: Sequential backbone assignments are obtained by NMR spectroscopy for a 1 MDa proteasome complex. The method relies on immobilization of a soluble protein complex by magic-angle spinning. Deuteration and proton detection of exchangeable sites and paramagnetic relaxation enhancement enables exploration of structural and dynamic properties of supramolecular assemblies at atomic resolution.
AU  - Mainz, A.
AU  - Religa, T.L.*
AU  - Sprangers, R.*
AU  - Linser, R.*
AU  - Kay, L.E.*
AU  - Reif, B.
C1  - 27455
C2  - 32678
SP  - 8746-8751
TI  - NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond.
JO  - Angew. Chem.-Int. Edit.
VL  - 52
IS  - 33
PB  - Wiley-VCH
PY  - 2013
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Second site: In the crystal structure of human MALT1casp-Ig3 (mucosa-associated lymphoid tissue lymphoma translocation protein 1) in complex with the tricyclic phenothiazine derivative thioridazine (violet in the picture), the inhibitor is bound in a hydrophobic pocket far from the active site. This explains the action of phenothiazine derivatives as noncompetitive, reversible inhibitors.
AU  - Schlauderer, F.*
AU  - Lammens, K.*
AU  - Nagel, D.
AU  - Vincendeau, M.
AU  - Eitelhuber, A.C.
AU  - Verhelst, S.H.*
AU  - Kling, D.*
AU  - Chrusciel, A.*
AU  - Ruland, J.*
AU  - Krappmann, D.
AU  - Hopfner, K.-P.*
C1  - 27786
C2  - 32812
SP  - 10384-10387
TI  - Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase.
JO  - Angew. Chem.-Int. Edit.
VL  - 52
IS  - 39
PB  - Wiley-VCH
PY  - 2013
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - There can be only one: Using a peptoid motif obtained by shifting the arginine side chain of a pentapeptide previously developed by Fujii et al. to the neighboring nitrogen atom restricts the conformational freedom and yields a conformationally homogeneous peptide (see picture) with a 100-fold higher binding affinity to the chemokine receptor CXCR4 in the picomolar range. Its efficiency to inhibit HIV-1 infections is also demonstrated. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
AU  - Demmer, O.*
AU  - Frank, A.O.*
AU  - Hagn, F.*
AU  - Schottelius, M.*
AU  - Marinelli, L.*
AU  - Cosconati, S.*
AU  - Brack-Werner, R.
AU  - Kremb, S.
AU  - Wester, H.J.*
AU  - Kessler, H.*
C1  - 8641
C2  - 30227
SP  - 8110-8113
TI  - A conformationally frozen peptoid boosts CXCR4 affinity and anti-HIV activity.
JO  - Angew. Chem.-Int. Edit.
VL  - 51
IS  - 32
PB  - Wiley-VCH
PY  - 2012
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Membrane proteins in their native cellular membranes are accessible by dynamic nuclear polarization magic angle spinning solid-state NMR spectroscopy without the need of purification and reconstitution (see picture). Dynamic nuclear polarization is essential to achieve the required gain in sensitivity to observe the membrane protein of interest.
AU  - Jacso, T.
AU  - Franks, W.T.*
AU  - Rose, H.*
AU  - Fink, U.*
AU  - Broecker, J.*
AU  - Keller, S.*
AU  - Oschkinat, H.*
AU  - Reif, B.
C1  - 7961
C2  - 29951
SP  - 432-435
TI  - Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution.
JO  - Angew. Chem.-Int. Edit.
VL  - 51
IS  - 2
PB  - Wiley-Blackwell
PY  - 2012
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Two-faced culprit: Fibrils of recombinantly produced amyloid β peptides (Aβs; residues 1–40) gave well-resolved solid-state NMR spectra. Two sets of resonances corresponding to residues 12–40 and 21–38 of the Aβ primary sequence were observed (see picture). Statistical analysis of electron microscopy data revealed that it was composed of a single Aβ polymorph, thus indicating that this Aβ fibril is composed of an asymmetric dimer.
AU  - Lopez del Amo, J.M.
AU  - Schmidt, M.*
AU  - Fink, U.*
AU  - Dasari, M.
AU  - Fändrich, M.*
AU  - Reif, B.
C1  - 7618
C2  - 29906
SP  - 6136-6139
TI  - An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
JO  - Angew. Chem.-Int. Edit.
VL  - 51
IS  - 25
PB  - Wiley-VCH 
PY  - 2012
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - The spread of antibiotic resistant bacteria is one of the most pressing problems in human health today. In the case of the opportunistic pathogen Pseudomonas aeruginosa, which causes lethal airway infections in cystic fibrosis and immunocompromised patients, the formation of biofilms plays an important role in antibiotic resistance and disease progression. Biofilm formation is mediated in part by the galactose-specific lectin LecA (PA-IL) and the fucose-specific lectin LecB (PA-IIL), as evidenced by studies with deletion mutants and the partial inhibitory effect of simple fucose and galactose derivatives in vitro and in vivo. Understanding the glycoconjugate–lectin interaction is a key feature in developing potent biofilm inhibitors. Capitalizing on the well-known cluster effect observed on binding of multivalent carbohydrates to lectins,  we recently reported the first case of P. aeruginosa biofilm inhibition with a multivalent lectin inhibitor, the fucosylated glycopeptide dendrimer FD2 (cFuc-Lys-Pro-Leu)4 (Lys-Phe-Lys-Ile)2Lys-His-IleNH2, which targets LecB. Herein we report the first case of P. aeruginosa biofilm inhibition with a multivalent ligand targeting the galactose-specific lectin LecA, using the related β-phenylgalactosyl peptide dendrimer GalAG2.
AU  - Kadam, R.U.*
AU  - Bergmann, M.*
AU  - Hurley, M.*
AU  - Garg, D.
AU  - Cacciarini, M.*
AU  - Swiderska, M.A.*
AU  - Nativi, C.*
AU  - Sattler, M.
AU  - Smyth, A.R.*
AU  - Williams, P.*
AU  - Cámara, M.*
AU  - Stocker, A.*
AU  - Darbre, T.*
AU  - Reymond, J.L.*
C1  - 6629
C2  - 29008
CY  - Weinheim, Germany
SP  - 10631-10635
TI  - A glycopeptide dendrimer inhibitor of the galactose-specific lectin LecA and of Pseudomonas aeruginosa biofilms.
JO  - Angew. Chem.-Int. Edit.
VL  - 50
IS  - 45
PB  - Verl. Chemie
PY  - 2011
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Structural characterization of insoluble proteins often relies on solid-state NMR spectroscopy. Perdeuteration and partial back-substitution of exchangeable protons, as proposed for crystalline model proteins, is now shown to lead to beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimer's disease β-amyloid peptide Aβ40, the lipid reconstituted β-barrel membrane protein OmpG, and the α-helical membrane protein bacteriorhodopsin. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
AU  - Linser, R.*
AU  - Dasari, M.
AU  - Hiller, M.*
AU  - Higman, V.*
AU  - Fink, U.*
AU  - Lopez del Amo, J.M.
AU  - Markovic, S.*
AU  - Handel, L.*
AU  - Kessler, B.*
AU  - Schmieder, P.*
AU  - Oesterhelt, D.*
AU  - Oschkinat, H.*
AU  - Reif, B.
C1  - 6242
C2  - 28864
SP  - 4508-4512
TI  - Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins.
JO  - Angew. Chem.-Int. Edit.
VL  - 50
IS  - 19
PB  - Wiley-Blackwell
PY  - 2011
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - no abstract
AU  - Madl, T.
AU  - Güttler, T.*
AU  - Görlich, D.*
AU  - Sattler, M.
C1  - 6245
C2  - 28866
SP  - 3993-3997
TI  - Structural analysis of large protein complexes using solvent paramagnetic relaxation enhancements.
JO  - Angew. Chem.-Int. Edit.
VL  - 50
IS  - 17
PB  - Wiley-Blackwell
PY  - 2011
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Sample preparation. A construct containing U2AF65 residues 148 to 342 (RRM12) was cloned into a modified pET9d vector containing an N-terminal His6-tag followed by a TEV protease cleavage site. Site-specific cysteine mutants were created individually at positions 155, 164, 171, 187, 188, 209, 273, 281, 287 and 318 by PCR amplification with overlapping oligonucleotides containing the mutated sequence, and afterwards verified by sequencing. Wild type and mutant U2AF65(RRM12) were produced in BL21(DE3) or BL21(DE3)pLysS cells using minimal M9T media supplemented with 2 g l-1 [13C]-glucose and/or 1 g l-1 [15N]- ammonium chloride. Following cell lysis, the proteins are purified by Ni2+ affinity chromatography resin in a buffer containing 50 mM Tris (pH 7.5), 500 mM NaCl, 5 % (v/v) glycerol with imidazole concentrations of 5, 30 and 250 mM for binding, wash and elution, respectively. The buffer was exchanged to phosphate buffered saline prior to removal of the His6-tag with 20 μg l-1 TEV protease. The His6-tag, uncleaved protein and TEV protease werre removed by Ni2+ affinity chromatography, and the final sample placed into 20 mM sodium phosphate (pH 6.5), 50 mM NaCl, 0.1% sodium azide and 1 mM EDTA. To make the samples for PRE measurement, the protein was completely reduced by the addition of 2 mM dithiothreitol, and extensively dialyzed in 50 mM Tris (pH 8.0) and 200 mM NaCl. Three molar equivalents of methanol-dissolved 3-(2-iodoacetamido)-2,2,5,5,tetramethyl-1- pyrrolidinyloxy radical (iodoacetamido-PROXYL; Sigma-Aldrich) was added and the reaction left in the dark at +4 °C for 16 hours. Unreacted spin label was removed following three changes of buffer into 20 mM sodium phosphate (pH 6.5), 50 mM NaCl, 0.1% sodium azide and 1 mM EDTA using a PD10 desalting column (GE Healthcare Life Sciences). The U9 RNA oligonucleotide was purchased from Biospring GmbH, Frankfurt (Germany) and dissolved into water.
AU  - Simon, B.*
AU  - Madl, T.
AU  - Mackereth, C.D.*
AU  - Nilges, M.*
AU  - Sattler, M.
C1  - 5660
C2  - 27929
CY  - Weinheim
SP  - 1967-1970
TI  - An efficient protocol for NMR-spectroscopy-based structure determination of protein complexes in solution.
JO  - Angew. Chem.-Int. Edit.
VL  - 49
IS  - 11
PB  - Wiley-VCH
PY  - 2010
SN  - 1433-7851
ER  - 

TY  - JOUR
AU  - Lenoir, D.
C1  - 2582
C2  - 23778
SP  - 3280-3284
TI  - Selektive Oxidation von organischen Verbindungen - nachhaltige katalytische Reaktionen mit Sauerstoff ohne Übergangsmetalle?
JO  - Angew. Chem.-Int. Edit.
VL  - 118
PY  - 2006
SN  - 1433-7851
ER  - 

TY  - JOUR
AU  - Lenoir, D.
C1  - 3591
C2  - 23708
SP  - 3206-3210
TI  - Selective oxidation of organic compounds - Sustainable catalytic reactions with oxygen and without transition metals?
JO  - Angew. Chem.-Int. Edit.
VL  - 45
PY  - 2006
SN  - 1433-7851
ER  - 

TY  - JOUR
AU  - Herges, R.*
AU  - Papafilippopoulos, A.*
AU  - Hess, K.*
AU  - Chiappe, C.*
AU  - Lenoir, D.
AU  - Detert, H.*
C1  - 1526
C2  - 22589
SP  - 1437-1441
TI  - cis-Bromierung von Alkinen ohne kationische Zwischenstufen.
JO  - Angew. Chem.-Int. Edit.
VL  - 117
PY  - 2005
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Surprising insight into a classical mechanism is provided by theoretical and experimental investigations on the bromination of alkynes. In nonpolar solvents the bromination of acetylene via a covalent tribromide adduct is strongly favored over the textbook mechanism via a bridged bromirenium ion. The structurally interesting intermediate explains the syn selectivity of the bromination of strained cycloalkynes.
AU  - Herges, R.*
AU  - Papafilippopoulos, A.*
AU  - Hess, K.*
AU  - Chiappe, C.*
AU  - Lenoir, D.
AU  - Detert, H.*
C1  - 1783
C2  - 22590
SP  - 1412-1416
TI  - cis-Bromination of Alkynes without cationic intermediates.
JO  - Angew. Chem.-Int. Edit.
VL  - 44
IS  - 9
PY  - 2005
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Aromatic substitution in detail: How does one prove that the intermediate charge-transfer (CT) complex (see scheme, where E=electrophile) is a key intermediate in the electrophilic substitution of arenes, and what is the structure, nature, and significance of this intermediate? On the basis of recent experimental findings these questions and others will be examined.
AU  - Lenoir, D.
C1  - 10367
C2  - 20995
SP  - 854-858
TI  - The electrophilic substitution of arenes : Is the Pi-complex a key intermediate and what is its nature?
JO  - Angew. Chem.-Int. Edit.
VL  - 42
PY  - 2003
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Bei Untersuchungen zur biologischen Dekontaminierung spielt der Weißfäulepilz eine große Rolle. Die ligin-Peroxidase dieses Pilzes katalysiert die Bildung von 3,3′,4,4′-Tetrachlorazobenzol 1 aus Dichloranilin. Da dieses hochtoxisches Produkt zu etwa 15% entsteht, müssen eingehende biochemische untersuchungen vor dem Einsatz des Pilzes in der Biotechnologie durchgeführt werden.
AU  - Pieper, D.H.
AU  - Winkler, R.
AU  - Sandermann, H.
C1  - 19550
C2  - 12651
SP  - 60-61
TI  - Bildung eines toxischen Dimerisierungsproduktes aus 3,4-Dichloranilin durch Lignin-Peroxidase von Phanerochaete chrysosporium.
JO  - Angew. Chem.-Int. Edit.
VL  - 104
IS  - 1
PY  - 1992
SN  - 1433-7851
ER  - 

TY  - JOUR
AU  - Pieper, D.H.
AU  - Winkler, R.
AU  - Sandermann, H.J.
C1  - 40649
C2  - 38916
SP  - 68-70
TI  - Formation of a toxic dimerization product of 3,4-Dichloroaniline by lignin peroxidase from Phanerochaete chrysosporium.
JO  - Angew. Chem.-Int. Edit.
VL  - 31
IS  - 1
PY  - 1992
SN  - 1433-7851
ER  - 

TY  - JOUR
AB  - Two zinc porphyrinate-modified Pt electrodes form the essential part of a very promising solar energy conversion system in which ultimately water is reduced to hydrogen. The Na//2 salt of ethylenediaminetetraacetic acid is employed as sacrificial electron donor; methyl viologen functions as electron transfer agent and platinized TiO//2 as reduction catalyst. Decisive is that the anode is coated with an n-semiconducting porphyrinate (zinc 5-(4-pyridyl)-10,15,20-tritolylporphyrinate) and the cathode with a p-semiconducting porphyrinate (zinc 5,10,15,20-tetra(4-pyridyl)porphyrinate).
AU  - Schuhmann, W.
AU  - Josel, H.P.
AU  - Parlar, H.A.
C1  - 42398
C2  - 36195
SP  - 241-243
TI  - New photosynthesis-like system for the light-induced reduction of water to molecular hydrogen.
JO  - Angew. Chem.-Int. Edit.
VL  - 26
IS  - 3
PY  - 1987
SN  - 1433-7851
ER  -