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Related Concept Videos

Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...

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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
12:07

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

The molybdenum cofactor.

Ralf R Mendel1

  • 1Department of Plant Biology, Braunschweig University of Technology, 38106 Braunschweig, Germany. r.mendel@tu-bs.de

The Journal of Biological Chemistry
|March 30, 2013
PubMed
Summary
This summary is machine-generated.

Molybdenum requires a special cofactor, the molybdenum cofactor (Moco), for catalytic activity in most enzymes. Its complex biosynthesis and distribution are essential for life, as deficiencies are lethal.

Keywords:
IronMetalloenzymesMetalloproteinsMetalsMolybdenum

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Molybdenum is a crucial transition element for numerous biological processes.
  • Catalytic activity of molybdenum enzymes depends on complexation with a unique pterin cofactor, forming the molybdenum cofactor (Moco).
  • Moco is essential for all molybdenum-containing enzymes except bacterial nitrogenase.

Purpose of the Study:

  • To elucidate the intricate biosynthesis pathway of the molybdenum cofactor (Moco).
  • To understand the essential components and steps involved in Moco synthesis.
  • To highlight the critical role of Moco in biological systems.

Main Methods:

  • The study describes the multi-step biosynthesis process of Moco.
  • It involves the interaction of six specific proteins.
  • The process requires additional cofactors such as iron, ATP, and copper.

Main Results:

  • The biosynthesis of Moco is a complex, four-step process.
  • Moco is subsequently distributed by Moco-binding proteins.
  • Successful Moco synthesis and distribution are vital for organism survival.

Conclusions:

  • The molybdenum cofactor (Moco) is indispensable for the function of most molybdenum enzymes.
  • The intricate biosynthesis and distribution mechanisms ensure Moco availability.
  • Disruptions in Moco biosynthesis lead to lethal outcomes, underscoring its fundamental importance.