The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine.
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Cosper MM, Jameson GN, Davydov R, Eidsness MK, Hoffman BM, Huynh BH, Johnson MK
The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine.
J Am Chem Soc. 2002 Nov 27;124(47):14006-7.
- PubMed ID
- 12440894 [ View in PubMed]
- Abstract
The combination of resonance Raman, electron paramagnetic resonance and Mossbauer 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.