Iron-sulfur cluster dynamics in biotin synthase: a new [2Fe-2S](1+) cluster - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Biochemical and Biophysical Research Communications Année : 2009

Iron-sulfur cluster dynamics in biotin synthase: a new [2Fe-2S](1+) cluster

Résumé

Biotin synthase (BioB) catalyses the final step in the biosynthesis of biotin. Aerobically purified biotin synthase contains one [2Fe-2S](2+) cluster per monomer. However, active BioB contains in addition a [4Fe-4S](2+) cluster which can be formed either by reconstitution with iron and sulfide, or on reduction with sodium dithionite. Here, we use EPR spectroscopy to show that mutations in the conserved YNHNLD sequence of Escherichia coli BioB affect the formation and stability of the [4Fe-4S](1+) cluster on reduction with dithionite and report the observation of a new [2Fe-2S](1+) cluster. These results serve to illustrate the dynamic nature of iron-sulfur clusters in biotin synthase and the role played by the protein in cluster interconversion.

Domaines

Chimie

Dates et versions

hal-00426282 , version 1 (23-10-2009)

Identifiants

Citer

Manuela Lotierzo, Bernadette Tse Sum Bui, Helen Leech, Martin Warren, Andrée Marquet, et al.. Iron-sulfur cluster dynamics in biotin synthase: a new [2Fe-2S](1+) cluster. Biochemical and Biophysical Research Communications, 2009, 381 (4), pp.487-490. ⟨10.1016/j.bbrc.2009.02.089⟩. ⟨hal-00426282⟩
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