Nitrosylation of 2Fe-2S and 4Fe-4S models for iron-sulphur redox proteins

Butler, Anthony R.; Glidewell, Christopher; Hyde, Andrew; Walton, John C.

doi:10.1016/s0020-1693(00)82246-x

Cited by 25 publications

(16 citation statements)

References 7 publications

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“…Enzymatic studies documenting the loss of iron-sulfur enzymatic function have supported this possibility further (64) and suggest close analogy to the CAM system reported here. The EPR properties of small molecular weight inorganic complexes containing iron-nitrosyl groups have been described (34)(35)(36)(39)(40)(41)(42)(43)(44)(45)(46), and these species exhibit spectra that are quite similar to those reported here. At the present time, it is unknown whether the species that gives rise to the spectra reported here is protein-bound or a smaller complex, perhaps similar in structure to Roussin's salts.…”

Section: Discussionsupporting

confidence: 73%

“…This result raises the possibility that at least part of the signal may be due to the presence of a small molecular weight complex of iron, nitric oxide, and thiolate anion-containing ligand(s). The EPR properties of such small molecular weight complexes have been described previously, and the spectra resemble those presented here (34)(35)(36)(39)(40)(41)(42)(43)(44)(45)(46), although the molecular nature of the species giving rise to these signals has not been delineated.…”

Section: Resultssupporting

confidence: 56%

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EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages.

Lancaster

Hibbs

1990

Proc. Natl. Acad. Sci. U.S.A.

476

218

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Activated macrophage cytotoxicity is characterized by loss of intracellular iron and inhibition of certain enzymes that have catalytically active nonheme-iron coordinated to sulfur. This phenomenon involves the oxidation of one of the terminal guanidino nitrogen atoms of L-arginine, which results in the production of citrulline and inorganic nitrogen oxides (NO-, NO5, and NO). We report here the results of an electron paramagnetic resonance spectroscopic study performed on cytotoxic activated macrophage (CAM) effector cells, which develop the same pattern of metabolic inhibition as their targets. Examination of activated macrophages from mice infected with Mycobacterium bovis (strain bacillus CalmetteGuerin) that were cultured in medium with lipopolysaccharide and L-arginine showed the presence of an axial signal at g = 2.039, which is similar to previously described iron-nitrosyl complexes formed from the destruction of iron-sulfur centers by nitric oxide (NO). Inhibition of the L-arginine-dependent pathway by addition of NG-monomethyl L-arginine (methyl group on a terminal guanidino nitrogen) inhibits the production of nitrite, nitrate, citrulline, and the g = 2.039 signal. Comparison of the hyperfine structure of the signal from cells treated with L-arginine with terminal guanidino nitrogen atoms of natural abundance N'4 atoms or labeled with N'5 atoms showed that the nitrosyl group in this paramagnetic species arises from one of these two atoms. These results show that loss of iron-containing enzyme function in CAM is a result of the formation of iron-nitrosyl complexes induced by the synthesis of nitric oxide from the oxidation of a terminal guanidino nitrogen atom of L-arginine.

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Section: Discussionsupporting

confidence: 73%

Section: Resultssupporting

confidence: 56%

EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages.

Lancaster

Hibbs

1990

Proc. Natl. Acad. Sci. U.S.A.

476

218

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“…The reaction of synthetic iron-sulfur clusters (both Fe 2 S 2 and Fe 4 S 4 ) with nitric oxide was first communicated in 1985 93. These studies demonstrated the propensity for cluster disassembly by NO gas and NO 2 − , but left unanswered the precise nature of the nitrosylation products.…”

Section: Fe2s2 Clustersmentioning

confidence: 99%

Detecting and Understanding the Roles of Nitric Oxide in Biology

2010

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We are pursuing a dual strategy for investigating the chemistry of nitric oxide as a biological signaling agent. In one approach, metal-based fluorescent sensors for the detection of NO in living cells are evaluated, and a sensor based on a copper fluorescein complex has proved to be a valuable lead compound. Sensors of this class permit identification of NO from both inducible and constitutive forms of nitric oxide synthase and facilitate investigation of different NO functions in response to external stimuli. In the other approach, we employ synthetic model complexes of ironsulfur clusters to probe their reactivity toward nitric oxide as biomimics of the active sites of ironsulfur proteins. Our studies reveal that NO disassembles the Fe-S clusters to form dinitrosyl iron complexes (DNICs).

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“…The ester can also be readily synthesized in v i m (Butler et. al., 1985b), and may cause -oesophagal cancer (Butler et al, 1985a). The decomposed ester is a much more potent nitrosation agent than the pure complex.…”

Section: Introductionmentioning

confidence: 99%

Interactions of iron-thiol-nitrosyl compounds with the phosphoroclastic system of Clostridium sporogenes

Payne¹,

Glidewell²,

Cammack³

1990

Journal of General Microbiology

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Certain reagents, such as ascorbate or iron salts and thiols, enhance the bacteriostatic action of nitrite on foodspoilage bacteria. This may be due to the formation of nitric oxide and iron-thiol4trosyl ((Fe-S-NO]) complexes. The minimum concentrations of these reagents required to inhibit growth of Clostridium sporogenes were investigated. A mixture of nitrite (0.72 mM) with iron (1.44 mM) and cystehe (2.16 mM) was found to be extremely inhibitory when autoclaved and diluted into the culture medium. This mixture caused rapid cessation of growth and loss of cell viability at a final concentration corresponding to 40 pM-nitrite. If added to the initial culture medium, it prevented growth at 5 pM-nitrite. The mixture W~S more inhibitory, on the basis of the nitrite concentration used, than the 'Perigo factor', obtained by autoclaving nitrite in growth medium. [Fe-%NO] compounds of known chemical structure were tested to determine if they were responsible for this effect. Total inhibition of cell growth was observed with the tetranuclear clusters [Fe,S,(NO),] (Roussin's black salt), [Fe,S,(NO),] or [Fe,Se,(NO),], added at concentrations equivalent to 10 pM-nitrite, or with [Fe2(SMe),(NO),] (methyl ester of Roussin's red salt), equivalent to 200 pM-nitrite. The rate of hydrogen production in growing cell cultures was inhibited by [Fe,S,(NO),] at levels equivalent to 2.5 pM-nitrite. EPR spectra of the inhibited cells showed features with g-values of 2-03, characteristic of mononuclear iron-nitrosyl species, and, under nonreducing conditions, an unusual signal at g = 1-65. There was no correlation between growth inhibition and the g = 2.03 signal, though there was a better correlation between inhibition and the g = 1.65 signal. The direct effects of the compounds were tested on the iron-sulphur proteins of the phosphoroclastic system, namely ferredoxin, pyruvate-ferredoxin oxidoreductase and hydrogenase. EPR spectra and enzyme assays showed that these proteins were not destroyed by [Fe,S,(NO),], [Fe,S,(NO),], [Fe,(SMe),(NO),], [Fe(SPh),(NO),], or M2 (an autoclaved mixture of 66 mM-cystehe, 3.6 mM-FeSO, and 0.72 m~-NaN0,) at concentrations higher than those that caused total inhibition of cell growth. Inhibition of cells by [Fe-S-NO] compounds is unlikely to be due to interaction with the preformed enzymes. The possible formation of iron-nitrosyl complexes in tritro, and their inhibitory actions, are discussed.

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Nitrosylation of 2Fe-2S and 4Fe-4S models for iron-sulphur redox proteins

Cited by 25 publications

References 7 publications

EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages.

EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages.

Detecting and Understanding the Roles of Nitric Oxide in Biology

Interactions of iron-thiol-nitrosyl compounds with the phosphoroclastic system of Clostridium sporogenes

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