Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli.

Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. Research Abstract Details 

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Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. Abstract Text:

Natalia B Ugulava,Kristene K Surerus,Joseph T Jarrett,

Biotin synthase is an AdoMet-dependent radical enzyme that catalyzes the insertion of an FeS cluster-derived sulfur atom into dethiobiotin. The dimeric enzyme is purified containing one [2Fe-2S]2+ cluster per monomer, but it is most active when reconstituted with an additional [4Fe-4S]2+ cluster per monomer. Using Mössbauer spectroscopy coupled with differential reconstitution of each cluster with 57Fe, we show that the reconstituted enzyme has approximately 1:1 [2Fe-2S]2+ and [4Fe-4S]2+ clusters and that the [4Fe-4S]2+ cluster is assembled at an alternate site not previously occupied by the [2Fe-2S]2+ cluster. These data suggest that biotin synthase is evolved to simultaneously accommodate two different clusters with unique roles in catalysis.

Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. Publishing Authors By Initials

NB Ugulava,KK Surerus,JT Jarrett,

For similar enzymes and coenzymes: enzymes: transferases: sulfur group transferases: sulfurtransferases research abstracts see: enzymes and coenzymes: enzymes: transferases: sulfur group transferases: sulfurtransferases research

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Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of the American Chemical Society

VOLUME: 124

Page Numbers: 9050-1

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 7

MONTH: Aug

YEAR: 2002

Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. Keywords Mesh Terms:

KEYWORDS: Sulfurtransferases

MESH TERMS: chemistry

Chemical & Substance for Abstract: Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. Information

Substance Name: biotin synthetase

Registry Number: EC 2.8.1.6

Grant and Affiliation Information for Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli.

AFFILIATION: Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01 GM059175-04

ACRONYM: GM

MEDLINETA: J Am Chem Soc

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