Mitochondria have Fe(III) receptors

J Weaver1, H Zhan, S Pollack

  • 1Department of Medicine, Albert Einstein College of Medicine, Bronx, NY 10461.

The Biochemical Journal
|January 15, 1990
PubMed

Insights

Adenosine triphosphate (ATP) is a key iron carrier in reticulocytes. Experiments show that ATP-iron complexes bind to specific mitochondrial receptors, influencing iron uptake and cellular processes.

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Iron Metabolism

Background:

  • Recent studies identify adenosine triphosphate (ATP) as the primary component of the low-molecular-weight iron pool in reticulocytes.
  • Understanding the interaction of iron complexes with cellular components is crucial for elucidating iron transport mechanisms.

Purpose of the Study:

  • To investigate the interaction between adenosine triphosphate-iron (ATP-Fe3+) complexes and mitochondria.
  • To characterize the binding affinity and specificity of iron complexes to mitochondrial receptors.

Main Methods:

  • Incubation of ATP-Fe3+ with isolated mitochondria.
  • Analysis of iron binding to mitochondrial receptors using varying iron chelators (PPi, nitrilotriacetate, citrate, ADP, GTP, AMP).
  • Assessment of binding saturation and reversibility.

Main Results:

  • ATP-Fe3+ demonstrated saturable and reversible binding to specific Fe3+ receptors on mitochondria.
  • Other iron complexes (PPi, nitrilotriacetate, citrate, ADP, GTP) also exhibited saturable binding.
  • Iron complexed to AMP, as well as Fe2+ complexes, showed non-specific binding.

Conclusions:

  • Mitochondria possess specific, high-affinity receptors for Fe3+ delivered via ATP.
  • The binding characteristics suggest a regulated mechanism for mitochondrial iron uptake involving specific iron chelators.
  • This interaction is vital for understanding iron homeostasis and ATP's role in reticulocyte iron metabolism.

Related Concept Videos

Electron Transport Chains01:28

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...
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,...
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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...
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,...
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,...