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The oxidative function of diferric transferrin.

Frederick L Crane¹, Hans Löw

¹Department of Biological Science, Purdue University, West Lafayette, IN 47907, USA.

Biochemistry Research International

|March 9, 2012

Summary

Diferric transferrin unexpectedly acts as a terminal oxidase, facilitating cytosolic NADH oxidation across the plasma membrane. This finding suggests novel roles in cell signaling and growth beyond iron uptake.

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Plasma membrane NADH oxidases are implicated in cellular signaling.
Transferrin's role has primarily been linked to iron uptake.

Purpose of the Study:

To investigate the unexpected role of diferric transferrin in cytosolic NADH oxidation.
To explore transferrin's function as a terminal oxidase for transplasma membrane NADH oxidase.

Main Methods:

Studies involving the reduction of iron in transferrin by plasma membrane NADH oxidase.
Analysis of NADH oxidation rates stimulated by diferric transferrin.

Main Results:

Diferric transferrin stimulates cytosolic NADH oxidation.

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The rapid reoxidation of transferrin iron under aerobic conditions suggests it does not primarily function in iron release for uptake at neutral pH.

Transferrin may act as a terminal oxidase or activate the plasma membrane NADH oxidase.

Conclusions:

Diferric transferrin plays an unexpected role as a terminal oxidase for transplasma membrane NADH oxidation.
This function may link to cell signaling, growth promotion independent of iron, and regulation of cytosolic NAD concentration.
Potential implications for sirtuin activation, aging, and growth control.