Thomas M. B. Reichhart

ORCID: 0000-0002-0538-108X
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About
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Research Areas
  • Electrochemical sensors and biosensors
  • Recreation, Leisure, Wilderness Management
  • Bacterial Genetics and Biotechnology
  • Urban Transport and Accessibility
  • Porphyrin Metabolism and Disorders
  • Urban Green Space and Health
  • Electrochemical Analysis and Applications
  • Analytical Chemistry and Sensors
  • Spectroscopy Techniques in Biomedical and Chemical Research
  • Hemoglobin structure and function
  • Advanced Electron Microscopy Techniques and Applications
  • Clostridium difficile and Clostridium perfringens research
  • Neonatal Health and Biochemistry
  • Land Use and Ecosystem Services
  • Advanced biosensing and bioanalysis techniques
  • Economic and Environmental Valuation
  • Photosynthetic Processes and Mechanisms
  • Enzyme Catalysis and Immobilization
  • Hyperglycemia and glycemic control in critically ill and hospitalized patients
  • Microfluidic and Capillary Electrophoresis Applications
  • Conducting polymers and applications

BOKU University
2007-2024

Max Planck Institute of Biophysics
2022-2024

Abstract Iron-bound cyclic tetrapyrroles (hemes) are redox-active cofactors in bioenergetic enzymes. However, the mechanisms of heme transport and insertion into respiratory chain complexes remain unclear. Here, we used cellular, biochemical, structural computational methods to characterize structure function heterodimeric bacterial ABC transporter CydDC. We provide multi-level evidence that CydDC is a required for functional maturation cytochrome bd , pharmaceutically relevant drug target....

10.1038/s41589-023-01314-5 article EN cc-by Nature Chemical Biology 2023-04-24

Abstract Cellobiose dehydrogenase (CDH) is capable of oxidizing cellobiose and related carbohydrates generating electrical current at carbon‐based electrodes through direct electron transfer (DET) or mediated (MET) mechanisms. As a result, CDHs have been utilized as biocatalysts in biosensors biofuel cell anodes. A novel engineered ascomycetous Class II CDH with enhanced glucose activity was tested bioelectrocatalyst for application to DET MET‐based the electrode component amount selection...

10.1002/celc.202200418 article EN cc-by ChemElectroChem 2022-06-06

Cellobiose dehydrogenase (CDH) is an attractive oxidoreductase for bioelectrochemical applications. Its two-domain structure allows the flavoheme enzyme to establish direct electron transfer biosensor and biofuel cell electrodes. Yet, application of CDH in these devices impeded by its limited stability under turnover conditions. In this work, we aimed improve semirational, high-throughput engineering. We screened 13 736 colonies a 96-well plate setup improved selected 11 variants. Measures...

10.1021/acssuschemeng.1c01165 article EN cc-by ACS Sustainable Chemistry & Engineering 2021-05-12

Abstract Research on implantable glucose biosensors is driven by the need for innovative medical devices continuous monitoring in patients with diabetes mellitus. However, biosensor sterilization a step that widely omitted during process of innovation. To compare effects gamma irradiation and chemical treatment ethylene oxide (carbon microarray electrodes are fabricated, functionalized oxidizing enzymes (cellobiose dehydrogenase CDH or oxidase GOx), coated specifically designed zwitterionic...

10.1002/adsr.202400056 article EN cc-by Advanced Sensor Research 2024-09-18

Abstract Cellobiose dehydrogenase (CDH) is a bioelectrocatalyst that enables direct electron transfer (DET) in biosensors and biofuel cells. The application of this bidomain hemoflavoenzyme for physiological glucose measurements limited by its acidic pH optimum slow interdomain (IET) at 7.5. reason rate‐limiting step electrostatic repulsion the interface between catalytic domain mediating cytochrome (CYT). We applied rational engineering to accelerate IET prevailing blood or interstitial...

10.1002/pro.4702 article EN cc-by Protein Science 2023-06-14

Managing blood glucose can affect important clinical outcomes during the intraoperative phase of surgery. However, currently available instruments for monitoring surgery are few and not optimized specific application. Here we report an attempt to exploit enzymatic sensor in a vein replica that could continuously monitor level authentic human bloodstream. First, detailed investigations superficial venous systems volunteers were carried out using ocular palpating examinations, as well advanced...

10.1016/j.bioelechem.2023.108441 article EN cc-by Bioelectrochemistry 2023-04-14

Abstract Iron-bound cyclic tetrapyrroles (hemes) are key redox-active cofactors in membrane-integrated oxygen reductases and other bioenergetic enzymes. However, the mechanisms of heme transport insertion into respiratory chain complexes remain unclear. Here, we used a combination cellular, biochemical, structural computational methods to resolve ongoing controversies around function heterodimeric bacterial ABC transporter CydDC. We provide multi-level evidence that CydDC is required for...

10.1101/2022.04.07.487047 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-04-07
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