Oliver Lenz

Oliver Lenz
Technische Universität Berlin | TUB · Department of Chemistry

Doctor (PhD)

About

175
Publications
17,451
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6,158
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Introduction
Faculty member conducting research in protein biochemistry and molecular biology. My group focus on the understanding of metalloenzymes catalyzing the conversion of hydrogen gas. Specialties: Basic research on gas-processing biocatalysts. Biotechnological application of hydrogenases that function in the presence of O2. Transition metal clusters involved in biocatalysis. Molecular genetics with proteobacteria. Hydrogen sensing in microorganisms.
Additional affiliations
November 2012 - present
Technische Universität Berlin
March 2008 - July 2008
Princeton University
January 1992 - October 2012
Humboldt-Universität zu Berlin

Publications

Publications (175)
Article
[NiFe] hydrogenases catalyze the reversible oxidation of molecular hydrogen into two protons and two electrons. A key organometallic chemistry feature of the NiFe active site is that the iron atom is co-coordinated by two cyanides (CN-) and one carbon monoxide (CO) ligand. Biosynthesis of the NiFe(CN-)2(CO) cofactor requires the activity of at leas...
Article
Full-text available
[NiFe]‐hydrogenases catalyze the reversible conversion of molecular hydrogen into protons end electrons. This reaction takes place at a NiFe(CN)2(CO) cofactor located in the large subunit of the bipartite hydrogenase module. The corresponding apo‐protein carries usually a C‐terminal extension that is cleaved off by a specific endopeptidase as soon...
Article
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Enzymes dependent on nicotinamide cofactors are important components of the expanding range of asymmetric synthetic techniques. New challenges in asymmetric catalysis are arising in the field of deuterium labelling, where compounds bearing deuterium (2H) atoms at chiral centres are becoming increasingly desirable targets for pharmaceutical and anal...
Article
Light-driven production of hydrogen by coupling natural photosystems or photosensitizers with hydrogen-producing catalysts has been achieved in numerous in vitro systems. Now, a recombinant in vivo system is described that generates hydrogen using a hydrogenase enzyme directly coupled to a cyanobacterial photosystem.
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Full-text available
Chemically synthesized compounds that are capable in the reversible splitting of dihydrogen into protons and electrons are rare in the chemists’ portfolio. The corresponding biocatalysts –hydrogenases– are, however, abundant in...
Preprint
[NiFe]-hydrogenases are biotechnologically relevant enzymes catalyzing the reversible splitting of H2 into 2 e– and 2 H+ under ambient conditions. Catalysis takes place at the heterobimetallic NiFe(CN)2(CO) center, whose multistep biosynthesis involves careful handling of two transition metals as well as potentially harmful CO and CN– molecules. He...
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Hydrogenases are biotechnologically relevant metalloenzymes that catalyze the reversible conversion of molecular hydrogen into protons and electrons. The O2-tolerant [NiFe]-hydrogenases from Cupriavidus necator (formerly Ralstonia eutropha) are of particular interest as they maintain catalysis even in the presence of molecular oxygen. However, to m...
Cover Page
Full-text available
Metalloenzymes In their Research Article on page 15854, Christian Lorent, Marius Horch, Lars Lauterbach, Ingo Zebger et al. explore redox intermediates of [NiFe]‐hydrogenases by an advanced experimental approach for solvated, lyophilized, and crystallized metalloenzymes.
Cover Page
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Metalloenzyme Im Forschungsartikel auf S. 15988 erforschen Christian Lorent, Marius Horch, Lars Lauterbach, Ingo Zebger et al. Redox‐Intermediate von [NiFe]‐Hydrogenasen durch einen experimentellen Ansatz für solvatisierte, lyophilisierte und kristallisierte Metalloenzyme.
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Iron–sulfur (Fe–S) centers are versatile building blocks in biological electron transfer chains because their redox potentials may cover a wide potential range depending on the type of the cluster and the specific protein environment. Resonance Raman (RR) spectroscopy is widely used to analyze structural properties of such cofactors, but it remains...
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Hydrogenases are abundant metalloenzymes that catalyze the reversible conversion of molecular H2 into protons and electrons. Important achievements have been made over the past two decades in the understanding of these highly complex enzymes. However, most hydrogenases have low production yields requiring many efforts and high costs for cultivation...
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Ein multifunktionaler Aufbau für In-situ-Spektroskopie an gasverarbeitenden Metalloenzymen ermöglicht die kontrollierte Einstellung von Redoxzuständen in verschiedenen Probenformen. So konnte der Nia-C-Zustand von [NiFe]-Hydrogenasen mit NRVS charakterisiert werden. Zudem wurden Einblicke in die reduktive Aktivierung der Enzyme erhalten, und ein zu...
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A profound mechanistic characterization of complex metalloenzymes requires a multitude of complementary techniques. In this context, we developed a new experimental setup allowing controlled preparation of catalytic intermediates for characterization by various spectroscopic techniques. The in situ monitoring of redox transitions by infrared spectr...
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In this work, we demonstrate that diazonium electrografting of biocompatible interfaces on transparent conducting oxide indium tin oxide (ITO) can be controlled and optimised to achieve low charge transfer resistance, allowing highly efficient electron transfer to an immobilised model enzyme, the oxygen‐tolerant [NiFe]‐hydrogenase from Ralstonia eu...
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The catalytic mechanism of [NiFe]-hydrogenases is subject of extensive research. Apart from at least four reaction intermediates of H2/H+ cycling, there is also a number of resting states, which are formed under oxidizing conditions. Although not directly involved in the catalytic cycle, knowledge of their molecular structure and reactivity is impo...
Article
[NiFe]-hydrogenases catalyze the reversible reaction H2 ⇄ 2H+ + 2e–. Their basic module consists of a large subunit, coordinating the NiFe(CO)(CN)2 center, and a small subunit that carries electron-transferring iron–sulfur clusters. Here, we report the in vitro assembly of fully functional [NiFe]-hydrogenase starting from the isolated large and sma...
Preprint
Full-text available
The catalytic mechanism of H<sub>2</sub> conversion by [NiFe]-hydrogenase is subject of extensive research. Apart from at least four reaction intermediates of H<sub>2</sub>/H<sup>+</sup> cycling, there is also a number of resting states, which are formed under oxidizing conditions. While not directly involved in the catalytic cycle, knowledge of th...
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Carbon fixation via the Calvin cycle is constrained by the side activity of Rubisco with dioxygen, generating 2-phosphoglycolate. The metabolic recycling of phosphoglycolate was extensively studied in photoautotrophic organisms, including plants, algae, and cyanobacteria, where it is referred to as photorespiration. While receiving little attention...
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Hydrogenases are complex metalloenzymes, showing tremendous potential as H2-converting redox catalysts for application in light-driven H2 production, enzymatic fuel cells and H2-driven cofactor regeneration. They catalyze the reversible oxidation of hydrogen into protons and electrons. The apo-enzymes are not active unless they are modified by a co...
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The O2 ‐tolerant NAD+‐reducing hydrogenase (SH) from Ralstonia eutropha ( Cupriavidus necator ) has already been applied in vitro and in vivo for H2‐driven NADH recycling in coupled enzymatic reactions with various NADH‐dependent oxidoreductases. To expand the scope for application in NADPH‐dependent biocatalysis, we introduced changes in the NAD+‐...
Preprint
Full-text available
Carbon fixation via the Calvin cycle is constrained by the side activity of Rubisco with dioxygen, generating 2-phosphoglycolate. The metabolic recycling of 2-phosphoglycolate, an essential process termed photorespiration, was extensively studied in photoautotrophic organisms, including plants, algae, and cyanobacteria, but remains uncharacterized...
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Background: The chemolithoautotrophic β-proteobacterium Ralstonia eutropha H16 (Cupriavidus necator) is one of the most studied model organisms for growth on H2 and CO2. R. eutropha H16 is also a biologically significant bacterium capable of synthesizing O2-tolerant [NiFe]-hydrogenases (Hyds), which can be used as anode biocatalysts in enzyme fuel...
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Hydrogenases are valuable model enzymes for sustainable energy conversion approaches using H2, but rational utilization of these base-metal biocatalysts requires a detailed understanding of the structure and dynamics of their complex active sites. The intrinsic CO and CN⁻ ligands of these metalloenzymes represent ideal chromophores for infrared (IR...
Article
The hydrogen-oxidizing “Knallgas” bacterium Ralstonia eutropha can thrive in aerobic and anaerobic environments and readily switches between heterotrophic and autotrophic metabolism, making it an attractive host for biotechnological applications including the sustainable H2-driven production of hydrocarbons. The soluble hydrogenase (SH), one out of...
Preprint
p> Chemicals labelled with the heavy hydrogen isotope deuterium (<sup>2</sup>H) have long been used in chemical and biochemical mechanistic studies, spectroscopy, and as analytical tracers. More recently, demonstration of selectively deuterated drug candidates that exhibit advantageous pharmacological traits has spurred innovations in metal-cataly...
Article
Solar-driven electrolysis enables sustainable production of molecular hydrogen (H2), which represents a cheap and carbon-free reductant. Knallgas bacteria like Ralstonia eutropha are able to split H2 to supply energy in form of ATP and NADH, which can be subsequently used to power reactions of interest. R. eutropha employs the Calvin-Benson-Bassham...
Article
The catalytic properties of hydrogenases are nature’s answer to the seemingly simple reaction H2 ⇌ 2H⁺ + 2e⁻. Members of the phylogenetically diverse subgroup of [NiFe] hydrogenases generally consist of at least two subunits, where the large subunit harbors the H2-activating [NiFe] site and the small subunit contains iron-sulfur clusters mediating...
Article
Surface-enhanced infrared absorption spectroscopy is used in situ to determine the electrochemical stability of organic interfaces deposited onto the surface of nanostructured, thin-film gold electrodes via the electrochemical reduction of diazonium salts. These interfaces are shown to exhibit a wide electrochemical stability window in both acetoni...
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[NiFe] hydrogenases catalyze the reversible splitting of H2into protons and electrons at a deeply buried active site. The catalytic center can be accessed by gas molecules through a hydrophobic tunnel network. While most [NiFe] hydrogenases are inactivated by O2, a small subgroup, including the membrane-bound [NiFe] hydrogenase (MBH) ofRalstonia eu...
Chapter
Dioxygen-tolerant [NiFe]-hydrogenases are defined by their ability to catalyze the reaction, H2 ⇌ 2H⁺ + 2e⁻ even in the presence of O2. Catalytic and probably also noncatalytic mechanisms protect their active sites from being inactivated by reactive oxygen species, which makes them attractive subjects of investigation from both fundamental and appl...
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The fluorescent biosensor Frex, recently introduced as a sensitive tool to quantify the NADH concentration in living cells, was characterized by time-integrated and time-resolved fluorescence spectroscopy regarding its applicability for in vivo measurements. Based on the purified sensor protein, it is shown that the NADH dependence of Frex fluoresc...
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Biocatalysts that mediate the H2-dependent reduction of NAD(+) to NADH are attractive from both a fundamental and applied perspective. Here we present the first biochemical and spectroscopic characterization of an NAD(+)-reducing [NiFe]‑hydrogenase that sustains catalytic activity at high temperatures and in the presence of O2, which usually acts a...
Article
In article number 1606265 Lars J. C. Jeuken and co-workers use a layer-by-layer assembly of lipid bilayers to multiply the surface concentration of electroactive membrane enzymes at electrodes. The interconnected membrane multilayers, akin to those of thylakoid membranes, create a material that exhibits a linear increase in bioelectrocatalytic acti...
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Multilayered or stacked lipid membranes are a common principle in biology and have various functional advantages compared to single-lipid membranes, such as their ability to spatially organize processes, compartmentalize molecules, and greatly increase surface area and hence membrane protein concentration. Here, a supramolecular assembly of a multi...
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Serial femtosecond crystallography requires reliable and efficient delivery of fresh crystals across the beam of an X-ray free-electron laser over the course of an experiment. We introduce a double-flow focusing nozzle to meet this challenge, with significantly reduced sample consumption, while improving jet stability over previous generations of n...
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The present study considers the ways in which redox enzyme modules are coupled in living cells for linking reductive and oxidative half-reactions, and then reviews examples in which this concept can be exploited technologically in applications of coupled enzyme pairs. We discuss many examples in which enzymes are interfaced with electronically cond...
Article
Hydrogenases are nature's key catalysts involved in both microbial consumption and production of molecular hydrogen. H2 exhibits a strongly bonded, almost inert electron pair and requires transition metals for activation. Consequently, all hydrogenases are metalloenzymes that contain at least one iron atom in the catalytic center. For appropriate i...
Article
Ralstonia eutropha is a hydrogen-oxidizing (“Knallgas”) bacterium that can easily switch between heterotrophic and autotrophic metabolism to thrive in aerobic and anaerobic environments. Its versatile metabolism makes R. eutropha an attractive host for biotechnological applications, including H2-driven production of biodegradable polymers and hydro...
Article
O2-tolerant [NiFe] hydrogenases are attractive biocatalysts for utilization in H2/O2 fuel cells, thereby reducing the amount of platinum-based catalysts. The O2-tolerant membrane-bound hydrogenases isolated from Ralstonia eutropha and Aquifex aeolicus, have been previously studied at planar electrodes. The design of a powerful enzymatic fuel cell,...
Article
[NiFe] hydrogenases are metalloenzymes catalyzing the reversible heterolytic cleavage of hydrogen into protons and electrons. Gas tunnels make the deeply buried active site accessible to substrates and inhibitors. Understanding the architecture and function of the tunnels is pivotal to modulating the feature of O2 tolerance in a subgroup of these [...
Article
NiFe] hydrogenases are metalloenzymes catalyzing the reversible heterolytic cleavage of hydrogen into protons and electrons. Gas tunnels make the deeply buried active site accessible to substrates and inhibitors. Understanding the architecture and function of the tunnels is pivotal to modulating the feature of O 2 tolerance in a subgroup of these [...
Article
Full-text available
The tolerance towards oxic conditions of O2-tolerant [NiFe] hydrogenases has been attributed to an unusual [4Fe-3S] cluster that lies proximal to the [NiFe] active site. Upon exposure to oxygen, this cluster converts to a superoxidised (5+) state, which is believed to secure the formation of the so-called Ni-B state that is rapidly reactivated unde...
Article
Free access to article until March 23 under: http://authors.elsevier.com/a/1SU653SNvbeHD0 A novel group of bacterial [NiFe]-hydrogenases is responsible for high-affinity H2 uptake from the troposphere, and is therefore thought to play an important role in the global H2 cycle. Here we present the first crystal structure at 2.85-Å resolution of such...
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Protein immobilization on electrodes is a key concept in exploiting enzymatic processes for bioelectronic devices. For optimum performance, an in-depth understanding of the enzyme-surface interactions is required. Here, we introduce an integral approach of experimental and theoretical methods that provides detailed insights into the adsorption of a...
Article
The Cover shows a new approach to biocatalysis involving enzymes on carbon particles as a heterogeneous catalyst for H2-driven hydrogenations. In their Full Paper, Reeve et al. demonstrate that these particles operate in unbuffered water, give high yields of phenylethanol from acetophenone, and are easy to separate and re-use. Reaction rate is enha...
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We describe a new approach to selective H2-driven hydrogenation that exploits a sequence of enzymes immobilised on carbon particles. We used a catalyst system that comprised alcohol dehydrogenase, hydrogenase and an NAD+ reductase on carbon black to demonstrate a greater than 98 % conversion of acetophenone to phenylethanol. Oxidation of H2 by the...