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1. 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

2. 2. Hydrogen development

3. Reversible Glutamate Coordination to High-Valent Nickel Protects the Active Site of a [NiFe] Hydrogenase from Oxygen

5. Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment

6. Frontispiece: Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes

7. Frontispiz: Ein neuer Aufbau zur Untersuchung der Struktur und Funktion von solvatisierten, lyophilisierten und kristallinen Metalloenzymen – veranschaulicht anhand von [NiFe]‐Hydrogenasen

8. Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes

9. Ein neuer Aufbau zur Untersuchung der Struktur und Funktion von solvatisierten, lyophilisierten und kristallinen Metalloenzymen – veranschaulicht anhand von [NiFe]‐Hydrogenasen

10. Shedding Light on Proton and Electron Dynamics in [FeFe] Hydrogenases

22. Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase

30. Rücktitelbild: Resonanz-Raman-Spektroskopie als Methode zur Untersuchung des aktiven Zentrums von Hydrogenasen (Angew. Chem. 19/2013)

31. Resonanz-Raman-Spektroskopie als Methode zur Untersuchung des aktiven Zentrums von Hydrogenasen

32. Back Cover: Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases (Angew. Chem. Int. Ed. 19/2013)

33. Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases

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