46 results on '"Horch, Marius"'
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2. Characterization of Frex as an NADH sensor for in vivo applications in the presence of NAD+ and at various pH values
3. Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment.
4. Understanding 2D-IR Spectra of Hydrogenases: A Descriptive and Predictive Computational Study.
5. Ein neuer Aufbau zur Untersuchung der Struktur und Funktion von solvatisierten, lyophilisierten und kristallinen Metalloenzymen – veranschaulicht anhand von [NiFe]‐Hydrogenasen.
6. Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes.
7. X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases.
8. Understanding the structure and dynamics of hydrogenases by ultrafast and two-dimensional infrared spectroscopy.
9. Rational redox tuning of transition metal sites: learning from superoxide reductase.
10. Hydrogen evolution by cobalt hangman porphyrins under operating conditions studied by vibrational spectro-electrochemistry.
11. An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2-Tolerant Hydrogenase.
12. Domain motions and electron transfer dynamics in 2Fe-superoxide reductase.
13. Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase.
14. Microporous polymer network films covalently bound to gold electrodes.
15. Reversible Active Site Sulfoxygenation Can Explain the Oxygen Tolerance of a NAD+-Reducing [NiFe] Hydrogenase and Its Unusual Infrared Spectroscopic Properties.
16. Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O2-tolerant NAD+-reducing [NiFe] hydrogenase.
17. Impact of the Iron–Sulfur Cluster Proximal to the Active Site on the Catalytic Function of an O2-Tolerant NAD+-Reducing [NiFe]-Hydrogenase.
18. Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase.
19. Resonance Raman Spectroscopy on [NiFe] Hydrogenase Provides Structural Insights into Catalytic Intermediates and Reactions.
20. Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases.
21. Resonanz-Raman-Spektroskopie als Methode zur Untersuchung des aktiven Zentrums von Hydrogenasen.
22. Combining Spectroscopy and Theory to Evaluate Structural Models of Metalloenzymes: A Case Study on the Soluble [NiFe] Hydrogenase from Ralstonia eutropha.
23. Revealing the Absolute Configuration of the CO and CN− Ligands at the Active Site of a [NiFe] Hydrogenase.
24. The Hydrogenase Subcomplex of the NAD.
25. Untersuchung des katalytischen Zentrums der O2-toleranten NAD+-reduzierenden [NiFe]-Hydrogenase von Ralstonia eutropha H16 mit In-situ-EPR- und -FTIR-Spektroskopie.
26. Probing the Active Site of an O2-Tolerant NAD+-Reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 by In Situ EPR and FTIR Spectroscopy.
27. Frontispiz: Ein neuer Aufbau zur Untersuchung der Struktur und Funktion von solvatisierten, lyophilisierten und kristallinen Metalloenzymen – veranschaulicht anhand von [NiFe]‐Hydrogenasen.
28. Frontispiece: Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes.
29. A Beginner's Guide to Thermodynamic Modelling of [FeFe] Hydrogenase.
30. Electrocatalysis by Heme Enzymes—Applications in Biosensing.
31. Back Cover: Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases (Angew. Chem. Int. Ed. 19/2013).
32. Rücktitelbild: Resonanz-Raman-Spektroskopie als Methode zur Untersuchung des aktiven Zentrums von Hydrogenasen (Angew. Chem. 19/2013).
33. Enzymatic and spectroscopic properties of a thermostable [NiFe]‑hydrogenase performing H2-driven NAD+-reduction in the presence of O2.
34. Investigation of the NADH/NAD+ ratio in Ralstonia eutropha using the fluorescence reporter protein Peredox.
35. Light-Induced Electron Transfer in a [NiFe] Hydrogenase Opens a Photochemical Shortcut for Catalytic Dihydrogen Cleavage.
36. Understanding the [NiFe] Hydrogenase Active Site Environment through Ultrafast Infrared and 2D-IR Spectroscopy of the Subsite Analogue K[CpFe(CO)(CN) 2 ] in Polar and Protic Solvents.
37. Reversible Glutamate Coordination to High-Valent Nickel Protects the Active Site of a [NiFe] Hydrogenase from Oxygen.
38. Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes.
39. Shedding Light on Proton and Electron Dynamics in [FeFe] Hydrogenases.
40. X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases.
41. An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O 2 -Tolerant Hydrogenase.
42. Electrochemical and Infrared Spectroscopic Studies Provide Insight into Reactions of the NiFe Regulatory Hydrogenase from Ralstonia eutropha with O2 and CO.
43. Impact of the iron-sulfur cluster proximal to the active site on the catalytic function of an O2-tolerant NAD(+)-reducing [NiFe]-hydrogenase.
44. Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O 2 -tolerant NAD + -reducing [NiFe] hydrogenase.
45. Revealing the absolute configuration of the CO and CN- ligands at the active site of a [NiFe] hydrogenase.
46. Probing the active site of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 by in situ EPR and FTIR spectroscopy.
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