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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...
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Magnetic interactions between metal sites in complex enzymes.

Biplab K Maiti1, Isabel Moura2, José J G Moura3

  • 1School of Sciences, Department of Chemistry, Cluster University of Jammu, Jammu, 180001, India. biplabmaiti@clujammu.ac.in.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|July 24, 2025
PubMed
Summary

Magnetic interactions between iron-sulfur clusters and transition metals are key to metalloenzyme function. Understanding these interactions in enzymes like hydrogenases and dehydrogenases aids bioinspired catalyst design.

Keywords:
Aldehyde oxidoreductaseCO dehydrogenaseElectron transferIron–sulfur centersMagnetic interactions[NiFe] Hydrogenase

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Enzymology

Background:

  • Metalloenzymes utilize transition metal centers and iron-sulfur (Fe/S) clusters for catalysis.
  • Magnetic interactions between these components are crucial for enzyme function, influencing electron transfer and redox behavior.

Purpose of the Study:

  • To review the role of magnetic interactions between Fe/S clusters and metal centers in key metalloenzymes.
  • To highlight examples such as [NiFe] hydrogenases, xanthine oxidase (XO) family, and carbon monoxide dehydrogenases (CODHs).

Main Methods:

  • Focus on understanding Fe/S-metal center interactions through advanced spectroscopic techniques.
  • Utilizes electron paramagnetic resonance (EPR) and theoretical modeling.

Main Results:

  • Fe/S clusters act as electron relays interacting with catalytic sites in [NiFe] hydrogenases.
  • Mononuclear molybdenum in XO enzymes is coupled to Fe/S clusters, modulating activity.
  • CODHs show magnetic communication between active sites and Fe/S clusters for CO2/CO conversion.

Conclusions:

  • Magnetic interactions are fundamental to metalloenzyme mechanisms and catalytic efficiency.
  • Insights guide the development of bioinspired catalysts and energy technologies.