Tomasz Maciej Borowski - Catalysis

Author Information

Tomasz Maciej Borowski is affiliated with the Jerzy Haber Institute of Catalysis and Surface Chemistry at the Polish Academy of Sciences, located at Niezapominajek 8, PL-30239 Krakow, Poland. His research primarily focuses on enzyme catalysis and reaction mechanisms, with a specific interest in Fe(II)/2-oxoglutarate dependent enzymes and other catalytic processes.

Research Contributions

Tomasz Maciej Borowski has made significant contributions to the field of catalysis and enzyme reaction mechanisms. In 2022, he published several impactful papers, including studies on the selectivity of enzyme reactions involving Fe(II)/2-oxoglutarate dependent enzymes, as well as methodologies for predicting enzyme reaction kinetics using QM-only and QM:MM approaches. His research also delves into the mechanistic studies of visible light-induced CO release and the biophysical properties of manganese superoxide dismutase. In 2021, Borowski’s work included investigations into allosteric cooperation in β-lactam binding, the substrate-binding cavity of hyoscyamine 6β-hydroxylase, and the properties of carbon thin films on nanobainitic steel.

Aliases

The author is known by several aliases, including T Borowski, T. Borowski, Tomasz Borowski, and Tomasz Maciej Borowski.

Publication and Citation Metrics

Metric	Value
Citation Count	3122
h-index	27
Paper Count	175

Publications:

Frontispiece: Properties of the Reactants and Their Interactions within and with the Enzyme Binding Cavity Determine Reaction Selectivities. The Case of Fe(II)/2‐Oxoglutarate Dependent Enzymes

DOI: 10.1002/chem.202281863

Year: 2022

Model Setup and Procedures for Prediction of Enzyme Reaction Kinetics with QM-Only and QM:MM Approaches.

DOI: 10.1007/978-1-0716-1767-0_10

Year: 2022

Properties of the reactants and their interactions within and with the enzyme binding cavity determine reaction selectivities. The case of Fe(II)/2-oxoglutarate dependent enzymes.

DOI: 10.1002/chem.202104106

Year: 2022

Mechanistic studies of visible light-induced CO release from a 3-hydroxybenzo[g]quinolone

DOI: 10.1039/d1ra07527f

Year: 2022

Allosteric cooperation in ß-lactam binding to a non-classical transpeptidase

DOI: 10.1101/2021.09.06.459080

Year: 2021

On substrate-binding cavity of hyoscyamine 6β-hydroxylase from devil's trumpet

DOI: 10.1107/s0108767321085779

Year: 2021

Substitution of histidine 30 by asparagine in manganese superoxide dismutase alters biophysical properties and supports proliferation in a K562 leukemia cell line

DOI: 10.1007/s00249-021-01544-2

Year: 2021

Formation of Nitrogen Doped Titanium Dioxide Surface Layer on NiTi Shape Memory Alloy

DOI: 10.3390/ma14061575

Year: 2021

Heat transfer investigations in a liquid that is mixed by means of a multi-ribbon mixer

DOI: 10.2478/pjct-2021-0019

Year: 2021

The Microstructure and Properties of Carbon Thin Films on Nanobainitic Steel

DOI: 10.1007/s11661-021-06453-9

Year: 2021

Can Physical Degradation Be Reversed?

How Do System Administrators Contribute to Computational Catalysis?

How Can Researchers Access Public Domain Resources?

What role do conferences play in the field of Catalysis?

How are Cluster Catalysts Synthesized?

How Should Contaminated Laboratory Equipment Be Decontaminated?

What Are the Consequences of Reduced MTHFR Activity?

How Do Local Correlation Methods Work?

How is Digestibility Measured?

What are Standard Reference Materials (SRMs)?

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