Abstract
The Azotobacter-type 7Fe ferredoxin from Bacillus schlegelii was active as an electron carrier in the reduction system of cyt. c consisting of NADPH, FNR and cytochrome c (cyt. c). The only [3Fe4S] cluster in the Fd molecule acts as the active site for the reduction of cyt. c. The activity of the ferredoxin once increased by 10, 20 and 20% by heat treatment at 60, 80 and 90°C, respectively. The increasing of the activity is caused by the interconversion of the [4Fe4S] cluster to the [3Fe4S] cluster with increasing of the [3Fe4S] cluster in the concentration.
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