Biological iron-sulfur clusters: Mechanistic insights from mass spectrometry

Crack, Jason C.; Brun, Nick E. Le

doi:10.1016/j.ccr.2021.214171

Cited by 14 publications

(7 citation statements)

References 137 publications

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“…Iron plays essential roles in biology due to its remarkable electronic, substrate-binding, and catalytic properties. − However, installing this redox-active d-block transition metal into client proteins and enzymes requires that nutrient iron enters the cell and traffics through it. Iron trafficking remains poorly characterized despite a half-century of investigations, due in large part to the inherent lability of iron trafficking complexes.…”

Section: Introductionmentioning

confidence: 99%

Labile Iron Pool of Isolated Escherichia coli Cytosol Likely Includes Fe-ATP and Fe-Citrate but not Fe-Glutathione or Aqueous Fe

et al. 2023

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The existence of labile iron pools (LFePs) in biological systems has been recognized for decades, but their chemical composition remains uncertain. Here, the LFeP in cytosol from Escherichia coli was investigated. Mossbauer spectra of whole vs lysed cells indicated significant degradation of iron-sulfur clusters (ISCs), even using an unusually gentle lysis procedure; this demonstrated the fragility of ISCs. Moreover, the released iron contributed to the non-heme high-spin Fe(II) species in the cell, which likely included the LFeP. Cytosol batches isolated from cells grown with different levels of iron supplementation were passed through a 3 kDa cutoff membrane, and resulting flowthrough-solutions (FTSs) were subjected to SEC-ICP-MS. Mossbauer spectroscopy was used to evaluate the oxidation states of standards. FTSs exhibited iron-detected peaks likely due to different forms of Fe-citrate and Fe-nucleotide triphosphate complexes. Fe-Glutathione (GSH) complexes were not detected using physiological concentrations of GSH mixed with either Fe(II) or Fe(III); Fe(II)-GSH was concluded not to be a significant component of the LFeP in E. coli under physiological conditions. Aqueous iron was also not present in significant concentrations in isolated cytosol and is unlikely a major component of the pool. Fe appeared to bind ATP more tightly than citrate, but ATP also hydrolyzed on the timescale of tens of hours. Isolated cytosol contained excess ligands that coordinated the added Fe(II) and Fe(III). The LFeP in healthy metabolically active cells is undoubtedly dominated by the Fe(II) state, but the LFeP is redox-active such that a fraction might be present as stable and soluble Fe(III) complexes especially under oxidatively stressed cellular conditions.

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Section: Introductionmentioning

confidence: 99%

Labile Iron Pool of Isolated Escherichia coli Cytosol Likely Includes Fe-ATP and Fe-Citrate but not Fe-Glutathione or Aqueous Fe

et al. 2023

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“…Most studies of the evolution of metalloenzymes have primarily focused on other geometrical characteristics of proteins, such as folds [237][238][239] (secondary structure) rather than the metals in proteins or their corresponding tertiary structures. 95,147,168,[240][241][242] It is interesting to note that several researchers, particularly geochemists, have developed various hypotheses linking mineral structures to the metal centers of specific enzymes. 63,153,154,163,[243][244][245][246][247][248][249][250][251] The fact of the enzyme-like activity of inorganic nanomaterials implies that metalloenzymes are probably derived from inorganic nanozymes with the same metal center.…”

Section: Discussionmentioning

confidence: 99%

“…Such inorganic enzymes also have some architectural links with another big family of enzymes, iron-sulfur proteins, with a cluster of multinuclear iron and inorganic sulfide, where the irons are coordinated by protein amino acid residues and sulfides with such a function. 89,[145][146][147] Linked to early Earth history, before the Great Oxidation Event, large amounts of carbon dioxide (CO 2 ) and methane (CH 4 ) were the dominant components of the primitive atmosphere, 148 with a considerable concentration of hydrogen peroxide, [149][150][151] particularly after the period of snowball earth. 152 The ocean at that time might have contained all of these transition metal sulphides and even selenide nanoparticles.…”

Section: Xiao-lan Huangmentioning

confidence: 99%

What are inorganic nanozymes? Artificial or inorganic enzymes

Huang¹

2022

New J. Chem.

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“…Therefore, this Fe-S-NO mechanism is considered to be the main factor inhibiting the growth of Clostridium spp. vegetative cells, and it can also be observed in aerobic and facultative pathogens associated with cured meat products [ 26 ]. The dinitric iron complex formed by NO binding to proteins is present in prokaryotic and eukaryotic cells, and iron–sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress [ 27 ].…”

Section: The Role Of Nitrite In Fermented Meat Productsmentioning

confidence: 99%

Research Progress of Nitrite Metabolism in Fermented Meat Products

Shen

Zeng

Kong

et al. 2023

Foods

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Nitrite is a common color and flavor enhancer in fermented meat products, but its secondary amines may transfer to the carcinogen N-nitrosamines. This review focuses on the sources, degradation, limitations, and alteration techniques of nitrite. The transition among NO3− and NO2−, NH4+, and N2 constitutes the balance of nitrogen. Exogenous addition is the most common source of nitrite in fermented meat products, but it can also be produced by contamination and endogenous microbial synthesis. While nitrite is degraded by acids, enzymes, and other metabolites produced by lactic acid bacteria (LAB), four nitrite reductase enzymes play a leading role. At a deeper level, nitrite metabolism is primarily regulated by the genes found in these bacteria. By incorporating antioxidants, chromogenic agents, bacteriostats, LAB, or non-thermal plasma sterilization, the amount of nitrite supplied can be decreased, or even eliminated. Finally, the aim of producing low-nitrite fermented meat products is expected to be achieved.

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Biological iron-sulfur clusters: Mechanistic insights from mass spectrometry

Cited by 14 publications

References 137 publications

Labile Iron Pool of Isolated Escherichia coli Cytosol Likely Includes Fe-ATP and Fe-Citrate but not Fe-Glutathione or Aqueous Fe

Labile Iron Pool of Isolated Escherichia coli Cytosol Likely Includes Fe-ATP and Fe-Citrate but not Fe-Glutathione or Aqueous Fe

What are inorganic nanozymes? Artificial or inorganic enzymes

Research Progress of Nitrite Metabolism in Fermented Meat Products

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