Ferredoxin degradation in growing Clostridium pasteurianum during periods of iron deprivation.

Clostridium pasteurianum was grown in batch cultures on media with an initial iron concentration of 10 micron. The uptake of iron and the synthesis of ferredoxin was followed. All the iron present in the medium was taken up by the cells before 50% of the final cell density was attained. The bacteria then continued to grow in the complete absence of exogenous iron. Ferrodoxin was synthesized during growth until the exogenous iron concentration dropped below 1 micron. During growth in the absence of iron ferredoxin was degraded with the result that at the end of growth the cells did not contain ferredoxin. The specific activity of the iron sulfur protein, pyruvate synthase (E.C. 1.2.7.1), remained constant during growth of C. pasteurianum in the absence of exogenous iron. This finding suggest that ferredoxin was used as an endogenous source of iron for the synthesis of essential iron proteins during periods of iron deprivation.