WorldCat Identities

Einsle, Oliver

Overview
Works: 62 works in 85 publications in 1 language and 1,950 library holdings
Roles: dgs, Author, Contributor, Other
Classifications: QP535.F4, 570
Publication Timeline
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Most widely held works by Oliver Einsle
Iron-sulfur clusters in chemistry and biology by Tracey A Rouault( )

5 editions published in 2014 in English and held by 1,074 WorldCat member libraries worldwide

This volume on iron-sulfur clusters includes chapters that cover the history of the discovery of iron-sulfur clusters in the 1960s to discoveries of their role in the enzyme, aconitase (1980s), and numerous other proteins. It explains basic chemistry principles, how microbes, plants, and animals synthesize these complex prosthetic groups, and why it is important to understand the chemistry and biogenesis of FeS proteins
Characterization, Properties and Applications : Volume 1: Characterization, Properties and Applications by Francesco Bonomi( )

2 editions published in 2017 in English and held by 460 WorldCat member libraries worldwide

Iron-sulfur clusters in chemistry and biology by Tracey A Rouault( )

3 editions published in 2017 in English and held by 39 WorldCat member libraries worldwide

This volume on iron-sulfur proteins includes chapters that describe the initial discovery of iron-sulfur proteins in the 1960s to elucidation of the roles of iron sulfur clusters as prosthetic groups of enzymes, such as the citric acid cycle enzyme, aconitase, and numerous other proteins, ranging from nitrogenase to DNA repair proteins. The capacity of iron sulfur clusters to accept and delocalize single electrons is explained by basic chemical principles, which illustrate why iron sulfur proteins are uniquely suitable for electron transport and other activities. Techniques used for detection and stabilization of iron-sulfur clusters, including EPR and Mossbauer spectroscopies, are discussed because they are important for characterizing unrecognized and elusive iron sulfur proteins. Recent insights into how nitrogenase works have arisen from multiple advances, described here, including studies of high-resolution crystal structures
Structure and function of cytochrome c nitrite reductase by Oliver F Einsle( )

3 editions published between 1999 and 2000 in English and held by 24 WorldCat member libraries worldwide

Crystallographic and mutational studies of bacterial cytochrome c peroxidases = Kristallografische und Mutagenese-Studien an bakteriellen Cytochrom c Peroxidasesn by Julian Seidel( )

1 edition published in 2011 in English and held by 17 WorldCat member libraries worldwide

Zusammenfassung: Cytochrome c peroxidases (Ccps) are reactive oxygen species (ROS) detoxifying enzymes that can be found in various Gram negative bacteria. They consist of two domains with one heme group each and catalyze the reduction of hydrogen peroxide two water. The delta proteobacterium Geobacter sulfurreducens possesses two copies of Ccp encoding genes (ccpA and macA). All known structures of cytochrome c peroxidases show an inactive and closed conformation in the oxidized state. The only exception is the enzyme of Nitrosomonas europaea exhibiting a constant open conformation, even in the oxidized state. Based on sequence alignments protein variants of CcpA and MacA were created and the structures were solved. The CcpA variants S134P and S134P/V135K showed a partially open enzyme regarding the active-side environment. Escherichia coli possesses an gene encoding for a predicted Ccp that has a third domain with an additional heme group (yhjA). The structure of the reduced YhjA was solved to a resolution of 2.8 A and shows the N-terminal extension with a His/Met coordinated heme group and an open active site
Structure of the Vanadium Nitrogenase of Azotobacter vinelandii and mechanistic insights into biological nitrogen fixation by Daniel Sippel( )

1 edition published in 2017 in English and held by 17 WorldCat member libraries worldwide

Structural characterisation of the methyltransferases SgvM and MrsA and the polyphosphate kinase MrPPK2-III by Florian Kemper( )

1 edition published in 2016 in English and held by 17 WorldCat member libraries worldwide

Crystal structure of CcmF : the cytochrome c maturation heme lyase by Anton Brausemann( )

1 edition published in 2017 in English and held by 17 WorldCat member libraries worldwide

Structural and functional characterization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae and YihU of the sulfoglycolysis pathway = Strukturelle und funktionelle Charakterisierung der Na+-translozierenden NADH:Ubichinon Oxidoreduktase aus Vibrio cholerae und YihU des Sulfoglycolysis-Stoffwechselweges by Georg Vohl( )

1 edition published in 2014 in English and held by 16 WorldCat member libraries worldwide

Zusammenfassung: The Na+-translocating NADH:quinone oxidoreductase, Na+-NQR, is a central respiratory enzyme of many pathogenic bacteria. Na+-NQR consists of six subunits called NqrA-NqrF and has a total molecular mass of 220 kDa. The function of Na+-NQR is similar to the one of complex I. It couples electron transfer from NADH to quinone with translocation of ions across the membrane to buildup a electrochemical gradient. However, Na+-NQR and complex I differ with respect to subunit number, cofactors bound, occurrence in organisms, and translocated ion. Complex I translocates H+, whereas the Na+-NQR pumps Na+. The Na+-NQR plays a central role in the sodium bioenergetics of many pathogenic bacteria, because the Na+ gradient is used for several important cellular processes; e.g. the movement of the flagellum and intake of nutrients are driven by the Na+ gradient. Moreover, Na+-NQR is linked to virulence gene expression in Vibrio cholerae. The fact that Na+-NQR is only found in prokaryotes makes it an ideal target for the development of new antibiotics. However, the exact reaction mechanism of the Na+-NQR is still unknown. In addition, there exists no published structural information about the whole complex that could help to better understand this enzyme. The main subject of the work was to improve the preliminary low resolution structural data of the entire Na+-NQR complex from V. cholerae, which were obtained within our group previously. For this, protein expression and purification protocols had to be optimized or newly established for the peripheric subunits NqrA and NqrC. Afterwards, these subunits were crystallized and the structures were determined at resolutions of 1.9 Å for NqrA and 1.7 Å for NqrC. The structure of NqrA revealed it as the first subunit of Na+-NQR that shares structural similarity to a subunit from complex I, Nqo1 from Thermus thermophilus. This was unexpected, because both subunits only have a low sequence identity. In addition, the structure of the NqrA indicates that Na+-NQR might have evolved from the Rhodobacter nitrogen fixation (RNF) complex. The structure of holo-NqrC is not similar to any known protein in the protein data bank except a homologue structure of apo-NqrC from Parabacteroides distasonis. NqrC contains a FMN that is covalently bound to Thr225 by a phosphoester bond and FMN located at the surface of the protein. The isoalloxazine moiety is oriented in the binding site in such a way that the C7 and C8 methyl groups are sticking out of the protein matrix. This might be essential for fast electron transfer. The high-resolution structures of NqrA and NqrC were used to complement the low-resolution structure of the entire complex, in which the electron density for the peripheric subunits was weak. In addition, the resolution of the Na+-NQR was improved from 3.5 to 3.2 Å by crystal optimization. The here presented structure of the Na+-NQR reveals several so far unknown features of the enzyme. The peripheric NqrC is located in the periplasm and not in the cytoplasm. A previously uncharacterized Fe within the membrane was found that is required for electron transfer across the membrane. Knowing the positions of the redox cofactors it was possible to predict an electron transfer pathway. A hypothesis how the Na+-translocation might be coupled to the electron transfer was suggested. However, even with the structural information present, the binding site of the terminal electron acceptor ubiquinone-8 still remains unknown. Through soaking of crystals from Na+-NQR the binding site of the inhibitor 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) was located at NqrB. It remains to be shown, whether this binding site represents the site of inhibition. In a second project YihU was structurally investigated. The reductase YihU of E. coli is part of the recently characterized sulfoglycolysis pathway, in which sulfoquinovose is degraded. Sulfoquinovose is the headgroup of sulfolipids found in plants, algae, and photosynthetic bacteria. YihU catalyzes the reduction of 3-sulfolactaldehyde to 2,3-dihydroxypropane-1-sulfonate (DHPS) under usage of NADH. DHPS is then used as a carbon source by other bacteria e.g. Cupriavidus pinatubonensi JMP134, which leads to a release of sulfate and thus closes the biological sulfur cycle. A protein expression and purification protocol was established for YihU. The protein was crystallized and the preliminary structure was determined at 1.3 Å. YihU forms a homodimer and is characterized by extensive domain swapping at the C-terminus. The domain swapping might be important for the regulation of the protein because it is occurring in close proximity to the proposed active site of the enzyme
The mechanism of NADH oxidation by respiratory complex I with focus on the production of reactive oxygen species by Emmanuel Gnandt( )

1 edition published in 2018 in English and held by 15 WorldCat member libraries worldwide

Abstract: The NADH:ubiquinone oxidoreductase, respiratory complex I, couples the transfer of electrons from NADH to ubiquinone with the translocation of four protons across a membrane. The mitochondrial complex I consists of 45 subunits, which the homologous bacterial one was shown to be composed of 13-15 subunits. 14 subunits are conserved in all organisms and represent the catalytic core subunits. The structures of the complex of bacteria and mitochondria is virtually identical. Thus, the bacterial enzyme represents a minimal structural model of mitochondrial complex I. Complex I oxidizes NADH by FMN and transfers the electrons to the quinone by a chain of seven (Fe-S)-clusters. An eighth cluster, located proximally to FMN, N1a, is conserved in the complex from all kingdoms of life, but not involved in the electron transfer to quinone. Hence, its role for catalysis remains enigmatic. The NADH oxidation site is susceptible of producing reactive oxygen species due to its solvent exposure. Complex I is known to be the major producer of cellular ROS and its dysfunction is associated with a multitude of severe diseases, such as the Leigh syndrome, a severe neurodegenerative disease. <br>In this work, the function of N1a should be identified by means of site-directed mutagenesis, enzymatic kinetics and structural analysis. Mutations found in patients suffering from Leigh syndrome should be introduced into bacterial complex I to identify the effects on structure and function. Finally, competitors to NADH binding should be identified that selectively inhibit ROS production.<br>Reduction of the peripheral cluster N1a could not be detected even using fast stopped-flow kinetics. However, EPR spectroscopy of samples that were generated by the ultra-fast freeze quenching revealed that the electron tunneling rates in a complex I variant containing N1a that cannot be reduced by NADH do not change. However, reduction of N1a regulates NADH binding. The rate of the complex I catalyzed activity is significantly diminished when the reation is initiated by an addition of ferricyanide instead of NADH. Detailled enzyme kinetics revealed that reduction of the (Fe-S)-clusters leads to a conformational change that in turn leaves the product NAD+ in its binding site blocking the access of NADH. This effect was not detectable in the variant with N1a that is not reducible by NADH. Thus, the reduction of N1a leads to a lower dissociation constant of NAD+. Structural investigations in our group revealed the local structural changes in the NADH binding site due to N1a reduction. Elimination of this mechanism by site-directed mutagenesis leads to an enhanced ROS production.<br>Furthermore, techniques were established to determine the thermal stability of proteins. They are based on the release of a fluorescent cofactor or the binding of a fluorescent marker. Several proteins were characterized by this methods revealing their complementarity. A novel buffer for the purification of complex I was established using these methods. <br>Mutations found in patients suffering from Leigh syndrome were introduced into E. coli complex I and the electron input modul of the compex from Aquifex aeolicus. The consequences of the mutations on the catalytic properties were tested with the E. coli variants and structural consequences were determined in the structure of the A. aeolicus modul. The mutations caused a reduced activity, an increase in H2O2 production, a change of the flavin midpoint potential and a reduced thermal stability of the enzyme, especially at the flavin site. It seems that Leigh syndrome is mainly caused by a reduced enzymatic activity paired with an increased H2O2 production. <br>To discover new structures that are possibly capable to reduce ROS production at the reduced FMN cofactor in complex I a combination of structure-based and fragment-based drug design with the highly specific complex I inhibitor NADH-OH as lead structure was used. Several possible binders were identified and their inhibitory effect on the NADH oxidase activity was determined. The structure of two compounds bound to NuoEF were successfully solved and identified a binding site within the NADH oxidation site. However, these compounds showed a low affinity to the complex
Resolving the ligand-binding to pattern recognition receptor for advanced glycation end products (RAGE) by Roya Tadayon( )

1 edition published in 2016 in English and held by 14 WorldCat member libraries worldwide

Abstract: The Receptor for Advanced Glycation Endproducts (RAGE) is a pattern recognition receptor and key in the innate immune response. It is a type 2 membrane protein with an ectodomain consisting of three immunoglobulin-like domains, V, C1, and C2 domain. RAGE activation triggers the initiation and perpetuation of the inflammatory response. Hyper-activation of RAGE is associated with chronic inflammatory disorders, diabetic complications, tumor outgrowth and neurodegenerative disorders. Wide varieties of structurally diverse ligands bind to RAGE and trigger intracellular signal cascades. The cellular response evoked upon RAGE-ligand interaction is dependent on the nature of the ligand, its concentration, and affinity towards the receptor. <br>In order to understand the molecular basis of receptor activation, I was studying the interaction of this unique receptor with several of its ligands. Key ligands of RAGE are Danger-Associated Molecular Pattern molecules (DAMPs) like e.g. S100A9, S100A12 and S100A8/A9. Using isothermal calorimetry, I have characterized binding of S100A9 to RAGE-VC1 tandem domain. Only the Ca2+- and Zn2+-bound form of S100A9 interacts with VC1. Analysis of the binding data suggests that the interaction at a Kd of 4 µM is largely entropy driven. Further I have characterized the interaction of S100 proteins with RAGE applying surface plasmon resonance and microscale thermophoresis. The X-ray structure of S100A9 in complex with Ca2+- and Zn2+ revealed drastic metal ion-induced conformational changes exposing hydrophobic pocket required for high-affinity RAGE binding. <br>Blocking the interaction of S100A9 with RAGE represents a promising pharmaceutical approach in the therapy of chronic inflammatory diseases. Therefore, I characterized the binding of new compounds which block S100A9-receptor interaction. I have analyzed a series of compounds from the Quinoline-3-carboxamides family (Q-compounds) by ITC and X-ray crystallography. Strikingly, all different compounds bound to the hydrophobic pocket of S100A9. The structural data presented here give first insights into the molecular mechanism of inhibition and provide the basis for the development of more potent and specific drugs in the future
The alternative NrfA of Campylobacter rectus by Simon Lukas Netzer( )

1 edition published in 2017 in English and held by 13 WorldCat member libraries worldwide

Structural characterization of the two copper proteins nitrous oxide reductase from Pseudomonas stutzeri and laccase Lcc5 from Coprinopsis cinerea by Anja Pomowski( )

1 edition published in 2011 in English and held by 13 WorldCat member libraries worldwide

Although, the reduction of nitrous oxide (N2O) is highly exergonic, a high activation barrier hinders a spontaneous reaction. With regard to inertness, N2O is second only to molecular nitrogen and in both cases a complex metal center is required for activation. The only known enzyme, which catalyzes the reduction of N2O to N2 is the oxygen sensitive copper-protein nitrous oxide reductase (N2OR). Crystallographic studies on this enzyme from Paracoccus denitrificans, Marinobacter hydrocarbonoclasticus and Achromobacter cycloclastes provided insight into its structure: The protein forms a head-to-tail homodimer, which was shown to be obligatory for enzyme reaction. Each monomer comprises of two distinct domains, an N-terminal ß-propeller with the tetranuclear CuZ site and a C-terminal cupredoxin-like domain carrying the mixed valent CuA center, similar to the one found in cytochrome c oxidase. However, these structures represent the aerobically isolated protein, which is only active upon extended incubation with reducing agents. In contrast, the purple form of nitrous oxide reductase from Pseudomonas stutzeri shows physiological activity without the necessity of reductive activation. This work presents the first structure of the purple form of nitrous oxide reductase and as well the first structure of a metal-N2O complex, providing new insights into the binding mode of N2O to the catalytic site. In pressurized crystals N2O binds between CuZ and CuA site, which is as previously described a mixed-valent center alternating between the oxidized mixed-valent [Cu+1.5:Cu+1.5] and the reduced [Cu+:Cu+] state thereby providing one electron per cycle. In contrast to previous structures, the histidine ligand of CuA1 is flexible and rotates to form hydrogen bonds with a near-by serine and aspartate residue in dependence of substrate binding
Phytoene Desaturase from Oryza sativa Oligomeric Assembly, Membrane Association and Preliminary 3D-Analysis by Sandra Sina Ellen Gemmecker( )

3 editions published between 2015 and 2016 in English and held by 6 WorldCat member libraries worldwide

Abstract: Recombinant phytoene desaturase (PDS-His6) from rice was purified to near-homogeneity and shown to be enzymatically active in a biphasic, liposome-based assay system. The protein contains FAD as the sole protein-bound redox-cofactor. Benzoquinones, not replaceable by molecular oxygen, serve as a final electron acceptor defining PDS as a 15-cis-phytoene (donor):plastoquinone oxidoreductase. The herbicidal PDS-inhibitor norflurazon is capable of arresting the reaction by stabilizing the intermediary FADred, while an excess of the quinone acceptor relieves this blockage, indicating competition. The enzyme requires its homo-oligomeric association for activity. The sum of data collected through gel permeation chromatography, non-denaturing polyacrylamide electrophoresis, chemical cross-linking, mass spectrometry and electron microscopy techniques indicate that the high-order oligomers formed in solution are the basis for an active preparation. Of these, a tetramer consisting of dimers represents the active unit. This is corroborated by our preliminary X-ray structural analysis that also revealed similarities of the protein fold with the sequence-inhomologous bacterial phytoene desaturase CRTI and other oxidoreductases of the GR2-family of flavoproteins. This points to an evolutionary relatedness of CRTI and PDS yielding different carotene desaturation sequences based on homologous protein folds
 
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WorldCat IdentitiesRelated Identities
Iron-sulfur clusters in chemistry and biology
Covers
Characterization, Properties and Applications : Volume 1: Characterization, Properties and ApplicationsIron-sulfur clusters in chemistry and biology
Alternative Names
Einsle, O. 1970-

Einsle, Oliver F. 1970-

Einsle, Oliver Florian 1970-

Oliver Einsle biochemicus

Oliver Einsle hulumtues

Oliver Einsle researcher

Languages
English (31)