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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • [FeFe]-hydrogenases and Mo-nitrogenase are unrelated enzymes with complex iron-sulfur cofactors.
  • Cofactor synthesis and insertion require specific maturation machinery.

Purpose of the Study:

  • To review recent insights into the biosynthetic pathways of [FeFe]-hydrogenase H-cluster and nitrogenase FeMo-cofactor.
  • To highlight similarities in the maturation processes of these complex cofactors.

Main Methods:

  • Review of recent scientific literature.
  • Comparative analysis of cofactor biosynthesis pathways.
  • Focus on radical SAM enzyme activity and cofactor assembly.

Main Results:

  • Emerging evidence reveals striking similarities in the maturation pathways of [FeFe]-hydrogenase H-cluster and nitrogenase FeMo-cofactor.
  • Radical SAM enzymes play a crucial role in modifying iron-sulfur cluster precursors on assembly scaffolds.
  • Cofactor maturation involves the synthesis and insertion of unique nonprotein ligands and culminates in cluster transfer to structural proteins.

Conclusions:

  • The maturation of [FeFe]-hydrogenase H-cluster and nitrogenase FeMo-cofactor share common paradigms, particularly involving radical SAM enzymes.
  • Nucleotide binding and hydrolysis are implicated in both systems, though their precise roles require further elucidation.
  • Understanding these shared pathways offers new perspectives on enzyme maturation and cofactor biosynthesis.