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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Electron Transport Chains

The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
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...
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...

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Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue
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Published on: March 23, 2015

Cytochrome c biogenesis in mitochondria.

P Giegé1, J M Grienenberger, G Bonnard

  • 1Institut de Biologie Moléculaire des Plantes du CNRS, Université Louis Pasteur, 12 rue du général Zimmer, 67084 Strasbourg, France.

Mitochondrion
|November 24, 2007
PubMed
Summary

Plant mitochondria utilize a unique Ccm protein pathway for heme attachment to c-type cytochromes, unlike the simpler mechanism in yeast and animals. This pathway involves nuclear and mitochondrial genes for essential electron transporters.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • C-type cytochromes are crucial electron transporters in the respiratory chain.
  • Their function relies on the covalent attachment of a heme prosthetic group.
  • Protein maturation involves heme attachment, a process known as biogenesis.

Purpose of the Study:

  • To investigate the distinct heme attachment pathway in plant mitochondria.
  • To understand the role of Ccm proteins in plant cytochrome c maturation.
  • To compare plant mitochondrial maturation with mechanisms in yeast and animals.

Main Methods:

  • Analysis of Ccm proteins encoded in plant nuclear and mitochondrial genomes.
  • Characterization of the heme delivery pathway involving Ccm proteins.
  • Identification of protein components including an ABC transporter, redox protein, and putative heme lyase.

Main Results:

  • Plant mitochondria possess a prokaryote-derived maturation pathway for c-type cytochromes.
  • This pathway involves a complex of Ccm proteins.
  • The Ccm protein system includes an ABC transporter, a redox protein, and a putative heme lyase.

Conclusions:

  • Plant mitochondria employ a sophisticated, ancestral heme delivery system for c-type cytochrome biogenesis.
  • This pathway differs significantly from the cytochrome c heme lyase system found in yeast and animals.
  • Understanding the Ccm protein pathway is vital for comprehending plant mitochondrial respiration.