A5004379895- Enzyme Catalysis and Immobilization
- Metalloenzymes and iron-sulfur proteins
- Electrocatalysts for Energy Conversion
- Advanced battery technologies research
- CO2 Reduction Techniques and Catalysts
- Microbial Metabolic Engineering and Bioproduction
- Chemical Synthesis and Analysis
- Enzyme Structure and Function
- Carbohydrate Chemistry and Synthesis
- Radical Photochemical Reactions
- Amino Acid Enzymes and Metabolism
- Advanced Photocatalysis Techniques
- Microbial Metabolism and Applications
- Biochemical and Molecular Research
- Catalysis for Biomass Conversion
- Chemical Reactions and Mechanisms
- Nanoplatforms for cancer theranostics
- Inorganic and Organometallic Chemistry
- Click Chemistry and Applications
- Organic Chemistry Cycloaddition Reactions
- Genomics and Phylogenetic Studies
- bioluminescence and chemiluminescence research
- Hydrogen Storage and Materials
- Metal-Catalyzed Oxygenation Mechanisms
- Structural and Chemical Analysis of Organic and Inorganic Compounds
Uppsala University
2019-2025
KTH Royal Institute of Technology
2012-2022
AlbaNova
2012-2022
Angstrom Designs (United States)
2020
Fundación Ciencias Exactas y Naturales
1970-1971
Hydrogenases are redox enzymes that catalyze the conversion of protons and molecular hydrogen (H2). Based on composition active site cofactor, monometallic [Fe]-hydrogenase is distinguished from bimetallic [NiFe]- or [FeFe]-hydrogenase. The latter has been reported with particularly high turnover activities for both H2 release oxidation, notably at neutral pH, ambient temperatures, negligible electric overpotential. Due to these properties, [FeFe]-hydrogenase represents "gold standard" in...
Microbial hydrogen (H2) cycling underpins the diversity and functionality of diverse anoxic ecosystems. Among three evolutionarily distinct hydrogenase superfamilies responsible, [FeFe] hydrogenases were thought to be restricted bacteria eukaryotes. Here, we show that anaerobic archaea encode diverse, active, ancient lineages through combining analysis existing new genomes with extensive biochemical experiments. are encoded by nine archaeal phyla expressed H2-producing Asgard archaeon...
One lock for different keys: A flexible arginine in the active site allows γ-aminobutyrate:pyruvate transaminases to bind chemically substrates L-alanine and γ-aminobutyric acid. Moreover, a residue facilitates promiscuous conversion of (S)-amines ketones. The degree promiscuity can be related distinct key amino acids lying at surface site. As service our authors readers, this journal provides supporting information supplied by authors. Such materials are peer reviewed may re-organized...
An efficient single-enzymatic cascade approach for the asymmetric synthesis of chiral amines has been developed, which applies amino donor 3-aminocyclohexa-1,5-dienecarboxylic acid spontaneously tautomerizing to reach reaction completion with excellent ee values.
A novel biocatalytic amine transaminase/acyl transferase cascade for the formation of amides in aqueous solution has been developed.
Artificial photosynthesis is seen as a path to convert and store solar energy into chemical for our society. In this work, highly fluorescent aspartic acid-based carbon dots (CDs) are synthesized employed photosensitizer drive photocatalytic hydrogen evolution with an [FeFe] hydrogenase (CrHydA1). The direct interaction in CDs from l-aspartic acid (AspCDs)/CrHydA1 self-assembly systems, which visualized native gel electrophoresis, has been systematically investigated understand the...
Digging in the database: Four synthetically useful transaminases for which no function was known were studied by evaluating a set of eight amino donors and seven acceptors (see figure). The four enzymes differ substantially their catalytic properties substrate preferences. We also used asymmetric synthesis range chiral amines observed excellent enantioselectivities conversions.
A semi-synthetic screening method for mining the biodiversity of [FeFe]-hydrogenases, expanding toolbox biocatalytic H<sub>2</sub>-gas production.
Characterization of a group D putative sensory [FeFe]-hydrogenase reveals how the active site can be tuned to decrease CO inhibition and increase stability reduced H-cluster while retaining ability catalyze H<sup>+</sup>/H<sub>2</sub> interconversion.
Studies of molecular catalysts traditionally aim at understanding how a certain mechanism allows the reaction to be fast. A distinct question, which has only recently received attention in case bidirectional catalysts, is much thermodynamic driving force required achieve fast catalysis either direction reaction. "Reversible" are that work way response even small departure from equilibrium and thus do not waste input free energy as heat; conversely, "irreversible" require large proceed an...
[FeFe] hydrogenases make up a structurally diverse family of metalloenzymes that catalyze proton/dihydrogen interconversion. They can be classified into phylogenetically distinct groups denoted A-G, which differ in structure and reactivity. Prototypical Group A have high turnover rates remarkable energy efficiency. As compared to enzymes, the putatively sensory D hydrogenase from Thermoanaerobacter mathranii (TamHydS) has thousand-fold lower H2 evolution rate overpotential requirement drive...
For biocatalytic production of pharmaceutically important chiral amines the ω-transaminase enzymes have proven useful. Engineering these has to some extent been accomplished by rational design, but mostly directed evolution. By use a homology model key point mutation in Chromobacterium violaceum was found upon comparison with engineered variants from homologous enzymes. The variant Trp60Cys gave increased specificity for (S)-1-phenylethylamine (29-fold) and 4′-substituted acetophenones...
Biohybrid technologies like semiartificial photosynthesis are attracting increased attention, as they enable the combination of highly efficient synthetic light-harvesters with self-healing and outstanding performance biocatalysis. However, such systems intrinsically complex, multiple interacting components. Herein, we explore a whole-cell photocatalytic system for hydrogen (H2) gas production model photosynthesis. The employed is based on Escherichia coli cells heterologously expressing...
Abstract ω‐Transaminases are a valuable class of enzymes for the production chiral amines with either ( R )‐ or S )‐configuration in high optical purity and 100% yield by biocatalytic reductive amination prochiral ketones. A versatile new assay was developed to quantify ω‐transaminase activity kinetic characterization enantioselectivity typing novel engineered based on conversion 1‐(6‐methoxynaphth‐2‐yl)alkylamines. The associated release acetonaphthone product can be monitored development...
Abstract A protein engineering approach for expanding the substrate scope of ( S )‐selective Chromobacterium violaceum amine transaminase is presented. Amino acid residues in small binding pocket active site were targeted order to increase size acceptance primary amines bearing two bulky groups. highly sensitive fluorescence assay was then used evaluate generated enzyme variants their activity towards propyl‐ and benzyl‐substituted screening substrates. The best variant, L59A/F88A,...
Biocatalysis is attracting interest in the chemical industry as a sustainable alternative large-scale transformations. However, low operational stability of naturally evolved enzymes challenge and major efforts are required to engineer protein stability, usually by directed evolution. The development methods for stabilization based on rational design great interest, it would minimize needed generate stable enzymes. Here we present strategy proline substitutions flexible areas identified...
[FeFe] hydrogenases, metalloenzymes catalyzing proton/dihydrogen interconversion, have attracted intense attention due to their remarkable catalytic properties and (bio-)technological potential for a future hydrogen economy. In order unravel the factors enabling efficient catalysis, both unique organometallic cofactors protein structural features, i.e., "outer-coordination sphere" effects been intensively studied. These structurally diverse enzymes are divided into distinct phylogenetic...
Abstract ATAs engineered for having an enlarged small binding pocket were applied the synthesis of enantiomerically pure ( R )‐benzo[1,3]dioxol‐5‐yl‐butylamine, a chiral component human leukocyte elastase inhibitor DMP 777 (L‐694,458). Kinetic resolution racemic amine was performed by using L59A variant S )‐selective ATA from Chromobacterium violaceum Cv ‐ATA), providing residual )‐enantiomer in excellent yield and >99% ee . At moderate enzyme loading absence co‐solvent, high volumetric...
Photobiocatalytic CO2 reduction represents an attractive approach for conversion of solar light and abundant resources to value-added chemicals. However, the design suitable systems requires a detailed understanding interaction between artificial photosensitizer biocatalyst interface. In this work, we investigate effect surfactant charge utilized in preparation phenoxazine-based organic molecule nanorods on with carbon monoxide dehydrogenase II from Carboxydothermus hydrogenoformans within...
[FeFe]-hydrogenases function as both H
Abstract Isobutene is a promising precursor for jet fuel due to its high energy density and favorable combustion properties. Light-driven bioproduction of isobutene has recently been investigated as an alternative strategy crude oil refinement or fermentation-based manufacturing processes by harnessing the unicellular cyanobacterium Synechocystis sp. PCC 6803 α-ketoisocaproate dioxygenase ( Rn KICD) from Rattus norvegicus . However, obtained production level was not sufficient, partially...