title: The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine.
abstract: The combination of resonance Raman, electron paramagnetic resonance and Mössbauer spectroscopies has been used to investigate the effect of S-adenosyl-l-methionine (SAM) on the spectroscopic properties of the [4Fe-4S]2+ cluster in biotin synthase. The results indicate that SAM interacts directly at a unique iron site of the [4Fe-4S]2+ cluster in BioB and support the hypothesis of a common inner-sphere mechanism for the reductive cleavage of SAM in the radical SAM family of Fe-S enzymes.
authors.affiliation: Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
authors.forename: Michele Mader
authors.initials: MM
authors.lastname: Cosper
authors.forename: Guy N L
authors.initials: GN
authors.lastname: Jameson
authors.forename: Roman
authors.initials: R
authors.lastname: Davydov
authors.forename: Marly K
authors.initials: MK
authors.lastname: Eidsness
authors.forename: Brian M
authors.initials: BM
authors.lastname: Hoffman
authors.forename: Boi Hanh
authors.initials: BH
authors.lastname: Huynh
authors.forename: Michael K
authors.initials: MK
authors.lastname: Johnson
mesh_terms: D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism; D012436:S-Adenosylmethionine / Q000737:chemistry* / Q000378:metabolism; D013059:Spectrum Analysis, Raman; D013466:Sulfurtransferases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D007506:Iron-Sulfur Proteins; D012436:S-Adenosylmethionine; D013466:Sulfurtransferases; C057985:biotin synthetase