NDLI: Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein

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Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein

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Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Crack, Jason C. Green, Jeffrey Johnson, Michael K. Subramanian, Sowmya Zhang, Bo Thomson, Andrew J. Le Brun, Nick E.
Description	Author Affiliation: Zhang B ( Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.);
Abstract	Fumarate and nitrate reduction (FNR) regulatory proteins are $O_{2}-sensing$ bacterial transcription factors that control the switch between aerobic and anaerobic metabolism. Under anaerobic conditions $[4Fe-4S]^{2+}-FNR$ exists as a DNA-binding homodimer. In response to elevated oxygen levels, the $[4Fe-4S]^{2+}$ cluster undergoes a rapid conversion to a $[2Fe-2S]^{2+}$ cluster, resulting in a dimer-to-monomer transition and loss of site-specific DNA binding. In this work, resonance Raman and UV-visible absorption/CD spectroscopies and MS were used to characterize the interconversion between $[4Fe-4S]^{2+}$ and $[2Fe-2S]^{2+}$ clusters in Escherichia coli FNR. Selective $^{34}S$ labeling of the bridging sulfides in the $[4Fe-4S]^{2+}$ cluster-bound form of FNR facilitated identification of resonantly enhanced $Cys^{32}S-^{34}S$ stretching modes in the resonance Raman spectrum of the $O_{2}-exposed$ $[2Fe-2S]^{2+}$ cluster-bound form of FNR. This result indicates $O_{2}-induced$ oxidation and retention of bridging sulfides in the form of $[2Fe-2S]^{2+}$ cluster-bound cysteine persulfides. MS also demonstrates that multiple cysteine persulfides are formed on $O_{2}$ exposure of $[4Fe-4S]^{2+}-FNR.$ The $[4Fe-4S]^{2+}$ cluster in FNR can also be regenerated from the cysteine persulfide-coordinated $[2Fe-2S]^{2+}$ cluster by anaerobic incubation with DTT and $Fe^{2+}$ ion in the absence of exogenous sulfide. Resonance Raman data indicate that this type of cluster conversion involving sulfide oxidation is not unique to FNR, because it also occurs in $O_{2}-exposed$ forms of $O_{2}-sensitive$ [4Fe-4S] clusters in radical S-adenosylmethionine enzymes. The results provide fresh insight into the molecular mechanism of $O_{2}$ sensing by FNR and iron-sulfur cluster conversion reactions in general, and suggest unique mechanisms for the assembly or repair of biological [4Fe-4S] clusters.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	39
Volume Number	109
Language	English
Publisher	National Academy of Sciences
Publisher Date	2012-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cysteine Chemistry Escherichia Coli Proteins Ferrous Compounds Iron-Sulfur Proteins Models, Chemical Oxygen Metabolism Spectrum Analysis Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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