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Iron–sulfur cluster dynamics in biotin synthase: A new [2Fe–2S]1+ cluster

Lotierzo, Manuela, Bui, Bernadette Tse Sum, Leech, Helen K., Warren, Martin J., Marquet, Andrée, Rigby, Stephen E. J. (2009) Iron–sulfur cluster dynamics in biotin synthase: A new [2Fe–2S]1+ cluster. Biochemical and Biophysical Research Communications, 381 (4). pp. 487-490. ISSN 0006-291X. (doi:10.1016/j.bbrc.2009.02.089) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:34295)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1016/j.bbrc.2009.02.089

Abstract

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.

Item Type: Article
DOI/Identification number: 10.1016/j.bbrc.2009.02.089
Subjects: Q Science > Q Science (General)
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Lin Riches
Date Deposited: 19 Jun 2013 13:04 UTC
Last Modified: 16 Nov 2021 10:11 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34295 (The current URI for this page, for reference purposes)

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