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Related Concept Videos

Activation Energy01:26

Activation Energy

Activation energy is the minimum amount of energy necessary for a chemical reaction to move forward. The higher the activation energy, the slower the rate of the reaction. However, adding heat to the reaction will increase the rate, since it causes molecules to move faster and increase the likelihood that molecules will collide. The collision and breaking of bonds represents the uphill phase of a reaction and generates the transition state. The transition state is an unstable high-energy state...
Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Enzymes and Activation Energy01:13

Enzymes and Activation Energy

The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to occur. During chemical reactions, certain chemical bonds break, and new ones form. For example, when a glucose molecule breaks down, bonds between the molecule's carbon atoms break. Since these are energy-storing bonds, they release energy when broken. However, the molecule must be somewhat contorted to get into a state that allows the bonds to...
Introduction to Mechanisms of Enzyme Catalysis01:13

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...
Enzymes and Activation Energy01:13

Enzymes and Activation Energy

The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to occur. During chemical reactions, certain chemical bonds break, and new ones form. For example, when a glucose molecule breaks down, bonds between the molecule's carbon atoms break. Since these are energy-storing bonds, they release energy when broken. However, the molecule must be somewhat contorted to get into a state that allows the bonds to...
Transition State Theory01:25

Transition State Theory

Transition-state theory, also known as activated-complex theory, provides a molecular-level explanation of reaction rates in both gas-phase and solution-phase reactions. It extends earlier kinetic models by considering the formation of a short-lived, high-energy configuration during a reaction.The progress of a chemical reaction can be represented using a reaction profile, which plots potential energy against the reaction coordinate. As two reactant molecules approach one another, their...

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Related Experiment Video

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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Published on: December 4, 2017

Dioxygen activation in methane monooxygenase: a theoretical study.

Benjamin F Gherman1, Mu-Hyun Baik, Stephen J Lippard

  • 1Department of Chemistry and Center for Biomolecular Simulation, Columbia University, New York, New York 10027, USA.

Journal of the American Chemical Society
|March 5, 2004
PubMed
Summary

This study details enzymatic dioxygen activation by soluble methane monooxygenase (MMOH) using advanced computational methods. It reveals a key pathway involving iron intermediates essential for methane oxidation catalysis.

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Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Enzymology

Background:

  • Soluble methane monooxygenase (MMOH) is crucial for methane oxidation, a key biogeochemical process.
  • Understanding the mechanism of dioxygen activation by MMOH is vital for catalysis research.
  • Previous theoretical studies have limitations in model size and quantitative accuracy.

Purpose of the Study:

  • To elucidate the atomic-level mechanism of enzymatic dioxygen activation by MMOH.
  • To identify the optimal reaction pathway and key intermediates.
  • To validate computational findings against experimental data.

Main Methods:

  • Broken-symmetry unrestricted Density Functional Theory (DFT) calculations.
  • Quantitative treatment of electron spins and couplings.
  • Extensive exploration of potential energy surfaces and determination of total energies.

Main Results:

  • Identified a detailed reaction pathway from diiron(II) to intermediate Q (di(μ-oxo)diiron(IV)).
  • Revealed the crucial role of a carboxylate shift involving Glu243.
  • Computed thermodynamic and kinetic parameters align with experimental observations.

Conclusions:

  • The study provides an accurate, atomistic description of MMOH's dioxygen activation mechanism.
  • The findings resolve discrepancies with prior theoretical investigations.
  • The computational approach offers a robust framework for studying metalloenzyme mechanisms.