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Catalysis

Catalysis

The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.

Catalysis

Catalysis

Catalysis influences the rate of chemical reactions by providing an alternative reaction pathway with lower activation energy. A catalyst speeds up a reaction, but it is not consumed during the process. The fundamental principle of catalysis is the ability of a catalyst to alter the reaction mechanism, often introducing a more efficient pathway than the uncatalyzed process.In a catalyzed reaction, the catalyst participates directly in the reaction mechanism. It interacts with reactants to form...

Heterogeneous Catalysis

Heterogeneous Catalysis

Heterogeneous catalysis involves a catalyst in a different phase from the reactants. It is a process where the catalyst and the reactants are in distinct phases, typically solid and gas or liquid.Most heterogeneous catalysts are metals, metal oxides, or acids. The list includes transition metals like iron (Fe), cobalt (Co), nickel (Ni), palladium (Pd), platinum (Pt), chromium (Cr), manganese (Mn), tungsten (W), silver (Ag), and copper (Cu). These metals possess partially vacant d orbitals that...

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...

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Related Experiment Video

Updated: Jul 10, 2026

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO₂ Reduction

Published on: April 10, 2018

Enzymatic catalysis on conducting graphite particles.

Kylie A Vincent¹, Xiang Li, Christopher F Blanford

¹Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QR, UK.

Nature Chemical Biology

|November 13, 2007

Summary

Enzyme pairs on conducting particles enable redox transformations. Hydrogenase and reductase enzymes on graphite microparticles facilitate nitrate or fumarate reduction using H2.

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Area of Science:

Biocatalysis
Electrochemistry
Enzyme Engineering

Background:

Enzyme-catalyzed redox reactions are crucial in biological systems.
Developing efficient artificial systems for redox transformations remains a challenge.
Immobilizing enzymes on conductive materials offers potential for enhanced catalytic activity.

Purpose of the Study:

To introduce a novel concept for enzyme-catalyzed redox transformations using enzyme pairs.
To demonstrate the feasibility of attaching electron donor and acceptor enzymes to conducting particles.
To investigate the catalytic efficiency of modified graphite microparticles for specific reductions.

Main Methods:

Modification of graphite microparticles with pairs of enzymes (hydrogenase and nitrate reductase or fumarate reductase).
Utilizing H2 as an electron donor for oxidation at one enzyme.
Employing the generated electrons for reduction reactions catalyzed by the second enzyme.

Main Results:

Successful immobilization of enzyme pairs onto conducting graphite microparticles.
Demonstrated catalytic activity of the modified particles in redox transformations.
Efficient reduction of nitrate or fumarate using H2 as the electron source.

Conclusions:

The proposed concept of enzyme pairs on conducting particles is effective for redox transformations.
Graphite microparticles serve as suitable supports for immobilizing enzyme systems.
This approach offers a promising strategy for artificial enzyme-catalyzed redox processes.