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

Brindley, Amanda A., Zajicek, Richard, Warren, Martin J. ORCID: https://orcid.org/0000-0002-6028-6456, Ferguson, Stuart J. and Rigby, Stephen E.J. (2010) NirJ, a radical SAM family member of the d1 heme biogenesis cluster. FEBS Letters, 584 (11). pp. 2461-2466. ISSN 0014-5793

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Abstract

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.

Item Type: Article
Additional Information: Funding Information: The financial support of the Biotechnological and Biological Sciences Research Council (BBSRC) in funding this research is gratefully acknowledged ( BBS/B/10323 ; BB/E022944 ; BB/D003997 ).
Uncontrolled Keywords: biosynthesis,heme d1,iron-sulfur centre,nirj,radical sam,tetrapyrrole,biophysics,structural biology,biochemistry,molecular biology,genetics,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1304
Faculty \ School: Faculty of Science
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Depositing User: LivePure Connector
Date Deposited: 20 Sep 2022 15:30
Last Modified: 03 Oct 2022 07:34
URI: https://ueaeprints.uea.ac.uk/id/eprint/88524
DOI: 10.1016/j.febslet.2010.04.053

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