Oliver Lenz
www.chemie.tu-berlin.de
0000-0003-4550-5128
Technische Universität Berlin
11 papers found
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Structural Determinants of the Catalytic Nia-L Intermediate of [NiFe]-Hydrogenase
Stepwise assembly of the active site of [NiFe]-hydrogenase
Frontispiz: Ein neuer Aufbau zur Untersuchung der Struktur und Funktion von solvatisierten, lyophilisierten und kristallinen Metalloenzymen – veranschaulicht anhand von [NiFe]‐Hydrogenasen
Frontispiece: Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes
Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production from Ralstonia eutropha H16 in Escherichia coli
Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes
Ein neuer Aufbau zur Untersuchung der Struktur und Funktion von solvatisierten, lyophilisierten und kristallinen Metalloenzymen – veranschaulicht anhand von [NiFe]‐Hydrogenasen
Hydroxy-bridged resting states of a [NiFe]-hydrogenase unraveled by cryogenic vibrational spectroscopy and DFT computations
In Vitro Assembly as a Tool to Investigate Catalytic Intermediates of [NiFe]-Hydrogenase
A membrane‐bound [NiFe]‐hydrogenase large subunit precursor whose C‐terminal extension is not essential for cofactor incorporation but guarantees optimal maturation
The large subunit of the regulatory [NiFe]-hydrogenase fromRalstonia eutropha– a minimal hydrogenase?
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