Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli

Sutton VR, Stubna A, Patschkowski T, Munck E, Beinert H, Kiley PJ (2004)
Biochemistry 43(3): 791-798.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
Sutton, V.R.; Stubna, A.; Patschkowski, ThomasUniBi; Munck, E.; Beinert, H.; Kiley, P.J.
Abstract / Bemerkung
The oxygen sensing ability of the transcription factor FNR depends on the presence of a [4Fe-4S]2+ cluster. In the presence of O2, conversion of the [4Fe-4S]2+ cluster to a [2Fe-2S]2+ cluster inactivates FNR, but the fate of the [2Fe-2S]2+ cluster in cells grown under aerobic conditions is unknown. The present study shows that the predominant form of FNR in aerobic cells is apo-FNR (cluster-less FNR) indicating that the [2Fe-2S]2+ cluster, like the [4Fe-4S]2+ cluster, is not stable under these conditions. By quantifying the amount of [2Fe-2S]2+ cluster in 2Fe-FNR in vitro in the presence of various reductants and oxidants (GSH, DTT, cysteine, O2, hydrogen peroxide, and superoxide), we found that superoxide, a byproduct of aerobic metabolism, significantly destabilized the [2Fe-2S]2+ cluster. Mössbauer spectroscopy was used to monitor the effects of superoxide on 2Fe-FNR in vivo; under cellular conditions that favored superoxide production, we observed the disappearance of the signal representative of the [2Fe-2S]2+ cluster. We conclude that the [2Fe-2S]2+ cluster of FNR is labile to superoxide both in vitro and in vivo. This lability may explain the absence of the [2Fe-2S]2+ cluster form of FNR under aerobic growth conditions.
Erscheinungsjahr
2004
Zeitschriftentitel
Biochemistry
Band
43
Ausgabe
3
Seite(n)
791-798
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1864105

Zitieren

Sutton VR, Stubna A, Patschkowski T, Munck E, Beinert H, Kiley PJ. Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli. Biochemistry. 2004;43(3):791-798.
Sutton, V. R., Stubna, A., Patschkowski, T., Munck, E., Beinert, H., & Kiley, P. J. (2004). Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli. Biochemistry, 43(3), 791-798. doi:10.1021/bi0357053
Sutton, V. R., Stubna, A., Patschkowski, T., Munck, E., Beinert, H., and Kiley, P. J. (2004). Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli. Biochemistry 43, 791-798.
Sutton, V.R., et al., 2004. Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli. Biochemistry, 43(3), p 791-798.
V.R. Sutton, et al., “Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli”, Biochemistry, vol. 43, 2004, pp. 791-798.
Sutton, V.R., Stubna, A., Patschkowski, T., Munck, E., Beinert, H., Kiley, P.J.: Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli. Biochemistry. 43, 791-798 (2004).
Sutton, V.R., Stubna, A., Patschkowski, Thomas, Munck, E., Beinert, H., and Kiley, P.J. “Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli”. Biochemistry 43.3 (2004): 791-798.

39 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Redox-Sensing Iron-Sulfur Cluster Regulators.
Crack JC, Le Brun NE., Antioxid Redox Signal 29(18), 2018
PMID: 28967283
PHB Biosynthesis Counteracts Redox Stress in Herbaspirillum seropedicae.
Batista MB, Teixeira CS, Sfeir MZT, Alves LPS, Valdameri G, Pedrosa FO, Sassaki GL, Steffens MBR, de Souza EM, Dixon R, Müller-Santos M., Front Microbiol 9(), 2018
PMID: 29599762
Mild hydrostatic pressure triggers oxidative responses in Escherichia coli.
Guyet A, Dade-Robertson M, Wipat A, Casement J, Smith W, Mitrani H, Zhang M., PLoS One 13(7), 2018
PMID: 30016375
Redox-sensing iron-sulfur cluster regulators.
Crack JC, Le Brun NE., Antioxid Redox Signal (), 2017
PMID: 29216742
Biochemical properties of Paracoccus denitrificans FnrP: reactions with molecular oxygen and nitric oxide.
Crack JC, Hutchings MI, Thomson AJ, Le Brun NE., J Biol Inorg Chem 21(1), 2016
PMID: 26790880
Fe-S proteins that regulate gene expression.
Mettert EL, Kiley PJ., Biochim Biophys Acta 1853(6), 2015
PMID: 25450978
Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans.
Pernikářová V, Sedláček V, Potěšil D, Procházková I, Zdráhal Z, Bouchal P, Kučera I., J Proteomics 125(), 2015
PMID: 25976748
Oxidative stress sensing by the iron-sulfur cluster in the transcription factor, SoxR.
Kobayashi K, Fujikawa M, Kozawa T., J Inorg Biochem 133(), 2014
PMID: 24332474
Oxygen sensing strategies in mammals and bacteria.
Taabazuing CY, Hangasky JA, Knapp MJ., J Inorg Biochem 133(), 2014
PMID: 24468676
Bacterial sensor kinases using Fe-S cluster binding PAS or GAF domains for O2 sensing.
Unden G, Nilkens S, Singenstreu M., Dalton Trans 42(9), 2013
PMID: 23138661
Bacterial iron-sulfur regulatory proteins as biological sensor-switches.
Crack JC, Green J, Hutchings MI, Thomson AJ, Le Brun NE., Antioxid Redox Signal 17(9), 2012
PMID: 22239203
Characterization of the [2Fe-2S] cluster of Escherichia coli transcription factor IscR.
Fleischhacker AS, Stubna A, Hsueh KL, Guo Y, Teter SJ, Rose JC, Brunold TC, Markley JL, Münck E, Kiley PJ., Biochemistry 51(22), 2012
PMID: 22583201
Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein.
Zhang B, Crack JC, Subramanian S, Green J, Thomson AJ, Le Brun NE, Johnson MK., Proc Natl Acad Sci U S A 109(39), 2012
PMID: 23019358
Phenotypic repertoire of the FNR regulatory network in Escherichia coli.
Tolla DA, Savageau MA., Mol Microbiol 79(1), 2011
PMID: 21166900
Ancient and essential: the assembly of iron-sulfur clusters in plants.
Balk J, Pilon M., Trends Plant Sci 16(4), 2011
PMID: 21257336
The role of the Fe-S cluster in the sensory domain of nitrogenase transcriptional activator VnfA from Azotobacter vinelandii.
Nakajima H, Takatani N, Yoshimitsu K, Itoh M, Aono S, Takahashi Y, Watanabe Y., FEBS J 277(3), 2010
PMID: 20067522
Bacterial sensors of oxygen.
Green J, Crack JC, Thomson AJ, LeBrun NE., Curr Opin Microbiol 12(2), 2009
PMID: 19246238
DNA-mediated redox signaling for transcriptional activation of SoxR.
Lee PE, Demple B, Barton JK., Proc Natl Acad Sci U S A 106(32), 2009
PMID: 19651620
Regulatory and structural differences in the Cu,Zn-superoxide dismutases of Salmonella enterica and their significance for virulence.
Ammendola S, Pasquali P, Pacello F, Rotilio G, Castor M, Libby SJ, Figueroa-Bossi N, Bossi L, Fang FC, Battistoni A., J Biol Chem 283(20), 2008
PMID: 18362154
The impact of O(2) on the Fe-S cluster biogenesis requirements of Escherichia coli FNR.
Mettert EL, Outten FW, Wanta B, Kiley PJ., J Mol Biol 384(4), 2008
PMID: 18938178
Iron-sulfur clusters as oxygen-responsive molecular switches.
Outten FW., Nat Chem Biol 3(4), 2007
PMID: 17372605
Mycobacterium tuberculosis WhiB3 responds to O2 and nitric oxide via its [4Fe-4S] cluster and is essential for nutrient starvation survival.
Singh A, Guidry L, Narasimhulu KV, Mai D, Trombley J, Redding KE, Giles GI, Lancaster JR, Steyn AJ., Proc Natl Acad Sci U S A 104(28), 2007
PMID: 17609386
Multiple superoxide dismutases in Agrobacterium tumefaciens: functional analysis, gene regulation, and influence on tumorigenesis.
Saenkham P, Eiamphungporn W, Farrand SK, Vattanaviboon P, Mongkolsuk S., J Bacteriol 189(24), 2007
PMID: 17921294
The superoxide dismutases of Bacillus anthracis do not cooperatively protect against endogenous superoxide stress.
Passalacqua KD, Bergman NH, Herring-Palmer A, Hanna P., J Bacteriol 188(11), 2006
PMID: 16707676
Transcription activation in vitro by the Bradyrhizobium japonicum regulatory protein FixK2.
Mesa S, Ucurum Z, Hennecke H, Fischer HM., J Bacteriol 187(10), 2005
PMID: 15866917
Kinetic analysis of the oxidative conversion of the [4Fe-4S]2+ cluster of FNR to a [2Fe-2S]2+ Cluster.
Sutton VR, Mettert EL, Beinert H, Kiley PJ., J Bacteriol 186(23), 2004
PMID: 15547274
Bacterial redox sensors.
Green J, Paget MS., Nat Rev Microbiol 2(12), 2004
PMID: 15550941

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 14730984
PubMed | Europe PMC

Suchen in

Google Scholar