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Updated: Aug 2, 2026

Multi-parameter Measurement of the Permeability Transition Pore Opening in Isolated Mouse Heart Mitochondria
Published on: September 7, 2012
Mitochondria have Fe(III) receptors
1Department of Medicine, Albert Einstein College of Medicine, Bronx, NY 10461.
Abstract:
Recent work has provided new evidence that ATP is the major constituent of the low-Mr iron pool in the reticulocyte. The interaction of the iron complex of ATP with mitochondria was investigated in the present experiments. When ATP-Fe3+ was incubated with mitochondria, Fe3+, free of ATP, bound with high affinity to Fe3+ receptors on the mitochondria. The binding was saturable and reversible. Iron which was complexed to PPi, nitrilotriacetate, citrate, ADP and GTP also showed saturable binding to mitochondria; Fe3+ complexed to AMP bound non-specifically, as did Fe2+/ascorbate complexed to AMP bound non-specifically, as did Fe2+/ascorbate and Fe2+/dithionite.
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.
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