STUDIES ON NON-HEME IRON PROTEINS AND PIERICIDIN A BINDING SITE OF SUBMITOCHONDRIAL PARTICLES FROM CANDIDA UTILIS CELLS GROWN IN MEDIA OF VARYING IRON CONCENTRATIONS

EPR spectra of iron sulfur proteins associated with succinate dehydrogenase, glycerol-1-phosphate dehydrogenase, NADH dehydrogenase, and, perhaps, the cytochromes b and c1 in submitochondrial particles from Candidautilis are presented. The piericidin A sensitive site is assigned to the oxygen side of the iron sulfur protein associated with NADH dehydrogenase. Virtually no correlation of piericidin A sensitivity with the EPR signal of the NADH dehydrogenase-linked iron sulfur protein is indicated from comparison of these parameters as a function of iron concentration in the growth medium. © 1969.