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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
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 |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 20 Sep 2022 15:30 |
| Last Modified: | 24 Oct 2022 06:53 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/88524 |
| DOI: | 10.1016/j.febslet.2010.04.053 |
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