Katarzyna P. Sokol

ORCID: 0000-0001-8631-8885
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About
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Research Areas
  • Photosynthetic Processes and Mechanisms
  • Microbial Fuel Cells and Bioremediation
  • Electrocatalysts for Energy Conversion
  • Electrochemical sensors and biosensors
  • Metalloenzymes and iron-sulfur proteins
  • Electrochemical Analysis and Applications
  • Advanced Photocatalysis Techniques
  • Cassava research and cyanide
  • CO2 Reduction Techniques and Catalysts
  • Spectroscopy and Quantum Chemical Studies
  • Catalytic Processes in Materials Science
  • Photoreceptor and optogenetics research
  • Sulfur Compounds in Biology
  • Copper-based nanomaterials and applications
  • Algal biology and biofuel production
  • Microbial Community Ecology and Physiology
  • Physical Education and Pedagogy
  • Mesoporous Materials and Catalysis
  • Molecular Junctions and Nanostructures
  • Electron Spin Resonance Studies
  • Ammonia Synthesis and Nitrogen Reduction
  • Photonic Crystals and Applications
  • Solar-Powered Water Purification Methods
  • TiO2 Photocatalysis and Solar Cells
  • Polymer Surface Interaction Studies

University of Cambridge
2016-2022

European Research Council
2022

Massachusetts Institute of Technology
2020

Nanyang Technological University
2015

A rational approach for a photosystem II-based electrode assembly is described, integrating redox polymers with high surface area hierarchically structured electrodes.

10.1039/c6ee01363e article EN cc-by Energy & Environmental Science 2016-01-01

Solar-driven coupling of water oxidation with CO2 reduction sustains life on our planet and is high priority in contemporary energy research. Here, we report a photoelectrochemical tandem device that performs photocatalytic to formate. We employ semi-artificial design, which wires W-dependent formate dehydrogenase (FDH) cathode photoanode containing the photosynthetic enzyme, Photosystem II, via synthetic dye complementary light absorption. From biological perspective, system achieves...

10.1021/jacs.8b10247 article EN cc-by Journal of the American Chemical Society 2018-11-19

Factors governing the photoelectrochemical output of photosynthetic microorganisms are poorly understood, and energy loss may occur due to inefficient electron transfer (ET) processes. Here, we systematically compare photoelectrochemistry photosystem II (PSII) protein-films cyanobacteria biofilms derive: (i) losses in light-to-charge conversion efficiencies, (ii) gains photocatalytic longevity, (iii) insights into ET mechanism at biofilm interface. This study was enabled by use...

10.1021/jacs.7b08563 article EN cc-by Journal of the American Chemical Society 2017-09-15

Hydrogenases (H2 ases) are benchmark electrocatalysts for H2 production, both in biology and (photo)catalysis vitro. We report the tailoring of a p-type Si photocathode optimal loading wiring ase through introduction hierarchical inverse opal (IO) TiO2 interlayer. This proton-reducing Si|IO-TiO2 |H2 is capable driving overall water splitting combination with photoanode. demonstrate unassisted (bias-free) by to modified BiVO4 photoanode photoelectrochemical (PEC) cell during several hours...

10.1002/anie.201805027 article EN cc-by Angewandte Chemie International Edition 2018-06-11

Semiartificial photosynthesis integrates photosynthetic enzymes with artificial electronics, which is an emerging approach to reroute the natural photoelectrogenetic pathways for sustainable fuel and chemical synthesis. However, reduced catalytic activity of in bioelectrodes limits overall performance further applications production. Here, we show new insights into factors that affect photoelectrogenesis a model system consisting photosystem II three-dimensional indium tin oxide graphene...

10.1021/acs.nanolett.8b04935 article EN cc-by Nano Letters 2019-01-28

Visible-light driven H2 evolution in water is achieved using catechol-photosensitised TiO2 nanoparticles with a molecular nickel catalyst. Layer-by-layer immobilisation of catechol-TiO2 onto tin-doped indium oxide electrodes generates photocathodic currents the presence an electron acceptor. This approach represents new strategy for controlling photocurrent direction dye-sensitised photoelectrochemical applications.

10.1039/c7cc05094a article EN cc-by Chemical Communications 2017-01-01

The biological formate hydrogenlyase (FHL) complex links a dehydrogenase (FDH) to hydrogenase (H2ase) and produces H2 CO2 from via mixed-acid fermentation in Escherichia coli. Here, we describe an electrochemical colloidal semiartificial FHL system that consists of FDH H2ase immobilized on conductive indium tin oxide (ITO) as electron relay. These vitro systems benefit the efficient wiring highly active enzyme pair allow for reversible conversion under ambient temperature pressure. hybrid...

10.1021/jacs.9b09575 article EN cc-by Journal of the American Chemical Society 2019-10-22

The origin of selectivity in the hollowing silica nanoparticles is investigated to further understand silica. It realized that, during synthesis, precursors are essentially ion‐paired polyelectrolytes, whose nucleation depends on concentration counter ions, and most importantly, size/length poly(silicic acid). Thus, “silica” that nucleates out at different stages synthesis has degrees ion doping, which explains its solubility water, microporosity, selective etching phenomena. water shown be...

10.1002/smll.201500539 article EN Small 2015-06-10

Direct potential control of protein redox centres for both electrochemical and EPR characterisation.

10.1039/c9cc03212f article EN Chemical Communications 2019-01-01

Protein film photoelectrochemistry has previously been used to monitor the activity of photosystem II, water-plastoquinone photooxidoreductase, but mechanistic information attainable from a three-electrode setup remained limited. Here we introduce four-electrode rotating ring disk electrode technique for quantifying light-driven reaction kinetics and pathways in real time at enzyme–electrode interface. This allows us study photochemical H2O oxidation II gain an in-depth understanding that...

10.1021/jacs.8b08784 article EN cc-by Journal of the American Chemical Society 2018-09-06

Thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions. In contrast to our knowledge TsdA activities, information on redox properties absence substrates is rather scant. To address this deficit, we combined magnetic CD (MCD) spectroscopy protein film electrochemistry (PFE) a study resolve heme ligation chemistry two representative TsdAs. We examined TsdAs from...

10.1074/jbc.ra119.010084 article EN cc-by Journal of Biological Chemistry 2019-08-30

Abstract Hydrogenases (H 2 ases) are benchmark electrocatalysts for H production, both in biology and (photo)catalysis vitro. We report the tailoring of a p‐type Si photocathode optimal loading wiring ase through introduction hierarchical inverse opal (IO) TiO interlayer. This proton‐reducing Si|IO‐TiO |H is capable driving overall water splitting combination with photoanode. demonstrate unassisted (bias‐free) by to modified BiVO 4 photoanode photoelectrochemical (PEC) cell during several...

10.1002/ange.201805027 article EN cc-by Angewandte Chemie 2018-06-11

The decahaem cytochrome MtrC from Shewanella oneidensis MR-1 was employed as a protein electron conduit between porous indium tin oxide electrode and redox enzymes. Using hydrogenase fumarate reductase, shown suitable efficient diode to shuttle electrons the with activity regulating direction of enzymatic reactions.

10.1039/c6cc02721k article EN cc-by Chemical Communications 2016-01-01

Abstract A growing number of bacterial species are known to move electrons across their cell envelopes. Naturally this occurs in support energy conservation and carbon-fixation. For biotechnology it allows electron exchange between bacteria electrodes microbial fuel cells during electrosynthesis. In context Rhodopseudomonas palustris TIE-1 is much interest. These respond light by taking from external environment, including electrodes, drive CO 2 -fixation. The PioA cytochrome, that spans the...

10.1088/1361-6528/ab92c7 article EN cc-by Nanotechnology 2020-05-13

Thiosulfate dehydrogenases are bacterial cytochromes that contribute to the oxidation of inorganic sulfur. The active sites these enzymes contain low-spin

10.1021/jacs.2c06062 article EN cc-by Journal of the American Chemical Society 2022-09-29
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