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Related Experiment Videos

Biotin synthase mechanism: an overview.

M Lotierzo1, B Tse Sum Bui, D Florentin

  • 1Synthèse, Structure et Fonction de Molécules Bioactives, UMR CNRS 7613, Université Paris VI, 4 place Jussieu, 75252 Paris Cedex 05, France.

Biochemical Society Transactions
|July 27, 2005
PubMed
Summary

Biotin synthase uses its iron-sulfur clusters to convert dethiobiotin into biotin. The (2Fe-2S) cluster likely donates the sulfur atom, and 9-mercaptodethiobiotin is an alternative substrate.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Radical SAM enzymes

Background:

  • Biotin synthase, a radical SAM enzyme, synthesizes biotin from dethiobiotin.
  • The enzyme utilizes two iron-sulfur clusters: (4Fe-4S) for electron transfer and (2Fe-2S) for sulfur transfer.
  • The precise sulfur source for biotin synthesis has been debated.

Purpose of the Study:

  • To elucidate the role of the (2Fe-2S) cluster in biotin synthesis.
  • To investigate the potential of 9-mercaptodethiobiotin as an alternative substrate.

Main Methods:

  • Reconstitution of the (2Fe-2S) cluster in apo-biotin synthase using various sulfur sources.
  • Enzymatic assays with dethiobiotin and 9-mercaptodethiobiotin using a defined in vitro system.

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Main Results:

  • Reconstitution experiments with isotopically labeled sulfur (34S, 35S) and selenium (Se2-) confirmed the (2Fe-2S) cluster as the sulfur donor.
  • 9-mercaptodethiobiotin was identified as an alternative substrate, yielding similar reaction rates and turnover as dethiobiotin.
  • Isotope transfer studies indicated the formation of a common intermediate from both substrates.

Conclusions:

  • The (2Fe-2S) cluster in biotin synthase is the direct sulfur donor for biotin synthesis.
  • 9-mercaptodethiobiotin serves as an efficient alternative substrate, suggesting a shared reaction pathway with dethiobiotin.