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Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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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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The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
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Enzyme Inhibition01:30

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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Introduction to Enzymes01:22

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Electron Transport Chains01:28

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Revealing the Ferroptotic Phenotype of Medulloblastoma
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Substrate interactions with human ferrochelatase.

Amy Medlock1, Larkin Swartz, Tamara A Dailey

  • 1Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 31, 2007
PubMed
Summary

Human ferrochelatase, crucial for heme synthesis, was structurally analyzed. Its crystal structure reveals the protoporphyrin IX substrate binds deeply within a closed active site pocket, offering mechanistic insights.

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Area of Science:

  • Biochemistry and Structural Biology
  • Enzymology and Heme Biosynthesis

Background:

  • Ferrochelatase is the final enzyme in heme biosynthesis, catalyzing iron insertion into protoporphyrin IX.
  • Human ferrochelatase is an inner mitochondrial enzyme featuring an essential [2Fe-2S] cluster and existing as a homodimer.

Purpose of the Study:

  • To elucidate the structural basis of human ferrochelatase activity.
  • To characterize the binding of the protoporphyrin IX substrate within the enzyme's active site.

Main Methods:

  • Determination of the crystal structure of human ferrochelatase.
  • Analysis of both substrate-bound ferrochelatase and a variant (R115L) lacking bound substrate at higher resolution.

Main Results:

  • The crystal structure reveals protoporphyrin IX bound deep within an enclosed active site pocket.
  • The bound porphyrin substrate is rotated ~100 degrees and buried ~4.5 A deeper compared to bacterial ferrochelatase.
  • The active site 'jaws' close upon substrate binding, completely engulfing the porphyrin.

Conclusions:

  • The substrate-binding mode suggests a mechanism involving deep burial and enclosure within the active site.
  • Structural insights provide a foundation for understanding ferrochelatase's catalytic mechanism and potential drug targeting.