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Christian Lorent

Naturwissenschaftler

Name	Christian Lorent
Zeit	2022 (Wirkungsdaten)
Ort	Berlin (Wirkungsort) Deutschland
Geschlecht	männlich
Akademischer Grad bzw. Titel	Dr. rer. nat.
Beruf	Naturwissenschaftler (charakteristischer Beruf)
Beziehung	Technische Universität Berlin. Fakultät Mathematik und Naturwissenschaften
Quelle	TU Homepage:: https://www.tu.berlin/vcard/christian.lorent
Datensatztyp	Person
GND-Nummer	1281050741
Datensatz-ID	1281050741
Beteiligt an alle anzeigen Lichtinduzierter Elektronentransfer in einer (NiFe)‐Hydrogenase: Eine Photochemische Abkürzung für die Katalytische Wasserstoffspaltung Light‐Induced Electron Transfer in a (NiFe) Hydrogenase Opens a Photochemical Shortcut for Catalytic Dihydrogen Cleavage Insights into electron transfer and bifurcation of the Synechocystis sp. PCC6803 hydrogenase reductase module Stabilizing monoatomic two-coordinate bismuth(I) and bismuth(II) using a redox noninnocent bis(germylene) ligand Stabilizing Monoatomic Two-Coordinate Bismuth(I) and Bismuth(II) Using a Redox Noninnocent Bis(germylene) Ligand In Vitro Assembly as a Tool to Investigate Catalytic Intermediates of [NiFe]-Hydrogenase Shedding Light on Proton and Electron Dynamics in [FeFe] Hydrogenases Crucial Role of the Chaperonin GroES/EL for Heterologous Production of the Soluble Methane Monooxygenase from Methylomonas methanica MC09 Catalytic and Spectroscopic Properties of the Halotolerant Soluble Methane Monooxygenase Reductase from Methylomonas methanica MC09 Catalytic and Spectroscopic Properties of the Halotolerant Soluble Methane Monooxygenase Reductase from Methylomonas methanica MC09 Combining electron paramagnetic resonance and vibrational spectroscopy to explore catalysis of hydrogen-converting enzymes Crucial role of the chaperonin GroES/EL for heterologous production of the soluble methane monooxygenase from Methylomonas methanica MC09 Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase From Cupriavidus necator in Escherichia coli X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases Changing the Reactivity of Zero‐ and Mono‐Valent Germanium with a Redox Non‐Innocent Bis(silylenyl)carborane Ligand Changing the Reactivity of Zero‐ and Mono‐Valent Germanium with a Redox Non‐Innocent Bis(silylenyl)carborane Ligand Ein neuer Aufbau zur Untersuchung der Struktur und Funktion von solvatisierten, lyophilisierten und kristallinen Metalloenzymen – veranschaulicht anhand von [NiFe]‐Hydrogenasen Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes Frontispiece: 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 Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production from Ralstonia eutropha H16 in Escherichia coli The large subunit of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha – a minimal hydrogenase? Kristallstruktur und Spektroskopie offenbaren einen Schwefel‐Liganden am aktiven Zentrum einer O 2 ‐stabilen (FeFe)‐Hydrogenase Caught in the H inact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O 2 ‐stable State of (FeFe) Hydrogenase Bis(silylene)‐Stabilized Monovalent Nitrogen Complexes X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by (NiFe) Hydrogenases Einelektronenübertragungsreaktionen in frustrierten und klassischen Silyliumion/Phosphan‐Lewis‐Paaren Single‐Electron Transfer Reactions in Frustrated and Conventional Silylium Ion/Phosphane Lewis Pairs

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Katalog der Deutschen Nationalbibliothek

Christian Lorent

Lichtinduzierter Elektronentransfer in einer (NiFe)‐Hydrogenase: Eine Photochemische Abkürzung für die Katalytische Wasserstoffspaltung

Light‐Induced Electron Transfer in a (NiFe) Hydrogenase Opens a Photochemical Shortcut for Catalytic Dihydrogen Cleavage

Insights into electron transfer and bifurcation of the Synechocystis sp. PCC6803 hydrogenase reductase module

Stabilizing monoatomic two-coordinate bismuth(I) and bismuth(II) using a redox noninnocent bis(germylene) ligand

Stabilizing Monoatomic Two-Coordinate Bismuth(I) and Bismuth(II) Using a Redox Noninnocent Bis(germylene) Ligand

In Vitro Assembly as a Tool to Investigate Catalytic Intermediates of [NiFe]-Hydrogenase

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

Crucial Role of the Chaperonin GroES/EL for Heterologous Production of the Soluble Methane Monooxygenase from Methylomonas methanica MC09

Catalytic and Spectroscopic Properties of the Halotolerant Soluble Methane Monooxygenase Reductase from Methylomonas methanica MC09

Catalytic and Spectroscopic Properties of the Halotolerant Soluble Methane Monooxygenase Reductase from Methylomonas methanica MC09

Combining electron paramagnetic resonance and vibrational spectroscopy to explore catalysis of hydrogen-converting enzymes

Crucial role of the chaperonin GroES/EL for heterologous production of the soluble methane monooxygenase from Methylomonas methanica MC09

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

High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase From Cupriavidus necator in Escherichia coli

X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases

Changing the Reactivity of Zero‐ and Mono‐Valent Germanium with a Redox Non‐Innocent Bis(silylenyl)carborane Ligand

Changing the Reactivity of Zero‐ and Mono‐Valent Germanium with a Redox Non‐Innocent Bis(silylenyl)carborane Ligand

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

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

Frontispiece: 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

Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production from Ralstonia eutropha H16 in Escherichia coli

The large subunit of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha – a minimal hydrogenase?

Kristallstruktur und Spektroskopie offenbaren einen Schwefel‐Liganden am aktiven Zentrum einer O 2 ‐stabilen (FeFe)‐Hydrogenase

Caught in the H inact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O 2 ‐stable State of (FeFe) Hydrogenase

Bis(silylene)‐Stabilized Monovalent Nitrogen Complexes

X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases

X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by (NiFe) Hydrogenases

Einelektronenübertragungsreaktionen in frustrierten und klassischen Silyliumion/Phosphan‐Lewis‐Paaren

Single‐Electron Transfer Reactions in Frustrated and Conventional Silylium Ion/Phosphane Lewis Pairs