Phosphine-mediated Heinz body formation and hemoglobin oxidation in human erythrocytes.

In this work the in vitro reactions of phosphine with intact red blood cells and membrane-free hemoglobin extracts are reported. We demonstrate that phosphine or phosphine derivatives induce dense aggregates of denatured hemoglobin known as 'Heinz bodies' in intact red blood cells. The reaction products include irreversible hemichrome formation. We further demonstrate an oxygen requirement for these effects. PH3 appears to act as a novel type of O2 radical chain initiator or propagator with heme proteins.