AI Article Synopsis

  • Biotin synthase only contains [2Fe-2S](2+) clusters when isolated under aerobic conditions.
  • Previous studies indicated that under reducing and anaerobic conditions, biotin synthase could be reconstituted with various iron-sulfur clusters including [4Fe-4S](2+) and [2Fe-2S](2+).
  • Using (57)Fe Mössbauer spectroscopy, it was found that aerobically grown cells contain a mix of [4Fe-4S](2+) and [2Fe-2S](2+) clusters, supporting the idea that both cluster types may play important roles in the enzyme's function.

Article Abstract

Biotin synthase, the enzyme that catalyzes the last step of the biosynthesis of biotin, contains only [2Fe-2S](2+) clusters when isolated under aerobic conditions. Previous results showed that reconstitution with an excess of FeCl(3) and Na(2)S under reducing and anaerobic conditions leads to either [4Fe-4S](2+), [4Fe-4S](+), or a mixture of [4Fe-4S](2+) and [2Fe-2S](2+) clusters. To determine whether any of these possibilities or other different cluster configuration could correspond to the physiological in vivo state, we have used (57)Fe Mössbauer spectroscopy to investigate the clusters of biotin synthase in whole cells. The results show that, in aerobically grown cells, biotin synthase contains a mixture of [4Fe-4S](2+) and [2Fe-2S](2+) clusters. A mixed [4Fe-4S](2+):[2Fe-2S](2+) cluster form has already been observed under certain in vitro conditions, and it has been proposed that both clusters might each play a significant role in the mechanism of biotin synthase. Their presence in vivo is now another argument in favor of this mixed cluster form.

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http://dx.doi.org/10.1021/bi026590qDOI Listing

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