Interaction of reactive oxygen and nitrogen species with albumin- and methemoglobin-bound dinitrosyl-iron complexes

Шумаев, К. Б.; Gubkin, A. A.; Сереженков, В. А.; Lobysheva, Irina; Kosmachevskaya, O. V.; Ruuge, E. K.; Ланкин, В. З.; Топунов, А. Ф.; Vanin, Anatoly F.

doi:10.1016/j.niox.2007.09.085

Cited by 85 publications

(62 citation statements)

References 26 publications

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“…Vanin and colleagues recently reported that an excess of superoxide can partially disrupt the DNIC in bovine albumin in vitro [43]. To test whether L-cysteine decomposes the protein-bound DNICs by promoting the production of superoxide and/or hydrogen peroxide under aerobic conditions, we included excessive amounts of superoxide dismutase and/or bovine liver catalase (Sigma co.) in the incubation solution.…”

Section: Resultsmentioning

confidence: 99%

Oxygen is required for the l-cysteine-mediated decomposition of protein-bound dinitrosyl–iron complexes

Yang

Duan

Landry

et al. 2010

Free Radical Biology and Medicine

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Increasing evidence suggests that iron-sulfur proteins are the primary targets of NO (nitric oxide). Exposure of Escherichia coli cells to NO readily converts iron-sulfur proteins to the protein-bound DNICs (dinitrosyl iron complexes). While the protein-bound DNICs are stable in vitro under aerobic or anaerobic conditions, they are efficiently repaired in aerobically growing E. coli cells even without new protein synthesis. The cellular repair mechanism for the NO-modified iron-sulfur proteins remains largely elusive. Here we report that unlike aerobically growing E. coli cells, the starved E. coli cells fail to re-activate the NO-modified iron-sulfur proteins. Significantly, addition of L-cysteine, but not other related biological thiols, results in decomposition of the protein-bound DNICs in the starved E. coli cells and in the cell extracts under aerobic conditions. However, L-cysteine has little or no effect on the protein-bound DNICs in the starved E. coli cells and in vitro under anaerobic conditions, suggesting that oxygen is required for the L-cysteine-mediated decomposition of the protein-bound DNICs. Additional studies reveal that L-cysteine is able to exchange the DNIC with the protein-bound DNICs to form the L-cysteine-bound DNIC which is rapidly disrupted by oxygen, resulting in eventual decomposition of the protein-bound DNICs under aerobic conditions.

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Section: Resultsmentioning

confidence: 99%

Oxygen is required for the l-cysteine-mediated decomposition of protein-bound dinitrosyl–iron complexes

Yang

Duan

Landry

et al. 2010

Free Radical Biology and Medicine

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show abstract

“…However, recent studies by Vanin and coworkers (53) demonstrated that DNICs (derived from GSH or cysteine) did not show any apoptotic activity in HeLa cells, in contrast to the pro-apoptotic effects of S-nitrosoglutathione (GSNO). These authors concluded that DNICs were bound to membrane proteins, as protein-bound DNICs had been shown to limit the reaction of NO with superoxide and the formation of toxic peroxynitrite (54).…”

Section: Role Of Dnics In Cytotoxicitymentioning

confidence: 99%

Nitrogen Monoxide (NO) Storage and Transport by Dinitrosyl-Dithiol-Iron Complexes: Long-lived NO That Is Trafficked by Interacting Proteins

Rahmanto

Kalinowski

Lane

et al. 2012

Journal of Biological Chemistry

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“…Interaction constant is about 10 7 M -1 sec -1 [10]. Antioxidant interactions between DNIC and other NO donors are also shown [7].…”

Section: Resultsmentioning

confidence: 83%

“…Previous investigations [8][9][10] showed that superoxide anion radical induces destruction of DNIC containing various ligands via oxidation of NO to peroxynitrite in these complexes. Interaction constant is about 10 7 M -1 sec -1 [10].…”

Section: Resultsmentioning

confidence: 97%

Possible Mechanism of Generation of Nitrite and Non-Thiolate Nitroso Compounds in Blood Plasma during Inflammatory Processes

et al. 2014

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Interaction of reactive oxygen and nitrogen species with albumin- and methemoglobin-bound dinitrosyl-iron complexes

Cited by 85 publications

References 26 publications

Oxygen is required for the l-cysteine-mediated decomposition of protein-bound dinitrosyl–iron complexes

Oxygen is required for the l-cysteine-mediated decomposition of protein-bound dinitrosyl–iron complexes

Nitrogen Monoxide (NO) Storage and Transport by Dinitrosyl-Dithiol-Iron Complexes: Long-lived NO That Is Trafficked by Interacting Proteins

Possible Mechanism of Generation of Nitrite and Non-Thiolate Nitroso Compounds in Blood Plasma during Inflammatory Processes

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