The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine.
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.
Cosper
Michele Mader
MM
Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
Jameson
Guy N L
GN
Davydov
Roman
R
Eidsness
Marly K
MK
Hoffman
Brian M
BM
Huynh
Boi Hanh
BH
Johnson
Michael K
MK
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
D007506:Iron-Sulfur Proteins; D012436:S-Adenosylmethionine; D013466:Sulfurtransferases; C057985:biotin synthetase