The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine.
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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.
author list (cited authors)
Cosper, M. M., Jameson, G., Davydov, R., Eidsness, M. K., Hoffman, B. M., Huynh, B. H., & Johnson, M. K
complete list of authors
Cosper, Michele Mader||Jameson, Guy NL||Davydov, Roman||Eidsness, Marly K||Hoffman, Brian M||Huynh, Boi Hanh||Johnson, Michael K