NirJ, a radical SAM family member of the d1 heme biogenesis cluster

Citations of this article
Mendeley users who have this article in their library.


NirJ is involved in the transformation of precorrin-2 into heme d1, although its precise role in the process has not been established. The purified protein was found to contain a 4Fe-4S centre, in line with the prediction that it belongs to the radical SAM class of enzymes. This was further confirmed by binding of S-adenosyl-l-methionine (SAM) to dithionite-reduced NirJ, which resulted in a decrease in the signal intensity and in a shift to higher field of the [4Fe-4S]1+ EPR signal. Significantly, though, this approach also led to the appearance of a small but reproducible organic radical signal that was associated with about 2% of the NirJ molecules and was affected by the incorporation of SAM deuterated at the 5' adenosyl group. © 2010 Federation of European Biochemical Societies.




Brindley, A. A., Zajicek, R., Warren, M. J., Ferguson, S. J., & Rigby, S. E. J. (2010). NirJ, a radical SAM family member of the d1 heme biogenesis cluster. FEBS Letters, 584(11), 2461–2466.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free