Complex Formation between Metallic Cations and Proteins, Peptides, and Amino Acids

Gurd, Frank R. N.; Wilcox, Philip E.

doi:10.1016/s0065-3233(08)60424-6

Cited by 322 publications

(112 citation statements)

References 246 publications

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“…Gurd (6) showed that copper ions catalyze the oxidation of sulfhydryl groups and formation of disulfide bridges. Krivis and Rabb (9) reported that the enhancement of antitubercular activity of Isoniazid by Cu (II) may actually be due to the formation of a Cu (I) complex.…”

Section: Discussionmentioning

confidence: 99%

Observations on the Mechanism of Copper Damage in Chlorella

1970

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Section: Discussionmentioning

confidence: 99%

Observations on the Mechanism of Copper Damage in Chlorella

1970

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“…L'histamine forme avec certains m6taux de transition des compos6s de coordination dont quelques propri6t6s physiologiques, pharmacologiques et biologiques importantes ont 6t6 mises en 6vidence par Gurd & Wilcox (1956), Andrews & Lyons (1957), Andrews, Lyons & O'Brien (1962) et Andrews & Romary (1964). En particulier, l'affinit6 sp6ciale que l'histamine des neurones, l'un des facteurs de r6gulation de la croissance cellulaire, pr6sente pour les m6taux canc6rig~nes, est signal6e par Hatem (1958Hatem ( ,1960.…”

Section: Introductionunclassified

Etude cristallographique du perchlorate de dihistamino-cuivre(II)

Bonnet¹,

Jeannin²

1970

Acta Crystallogr Sect B

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(Refu le 10 mars 1969) Dihistaminocopper(II) perchlorate, Cu(C6HsN3)2(C104)2, crystallizes in the monoclinic system: a= 8.235 + 0-006, b = 13.676 + 0-009, c= 8.084 + 0.006 A, p= 100 ° 5' + 5' and Z= 2; space group P21/c. 1099 independent (hkl) reflexions of a single crystal, shaped like a truncated pyramid, have been measured at room temperature. Convergent refinement by the full-matrix least-squares method, with anisotropic temperature factors, led to a weighted R index of 9"4% including zero reflexions. Two histamine molecules are chelated to one copper atom, each one being bound by two nitrogen atoms, one -N(1)-belonging to the imidazole ring and one -N(3)H2 belonging to the side chain. Perchlorate ions build chains parallel to the a axis; they are 'semi-coordinated' to the copper atom of a complex ion

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“…Some studies have demonstrated that Fe(II) at low concentrations is toxic to anaerobic bacteria such as anoxygenic phototrophs (19) or streptococci (20). Several possibilities for anaerobic Fe(II) toxicity include inhibition of the F-ATPase (20), binding to membranes (21), disruption of protein stability or replacement of active-site metal cofactors (22), and oxidation and precipitation of insoluble Fe(III) on cellular components to impair nutrient uptake (13). Under NDFO conditions, redox transformations of nitrogen oxides can produce intermediates, such as nitric oxide (NO), which is capable of binding to and reacting with heme cofactors (23) or Fe-S clusters (24) or, in the presence of transition metals, nitrosating protein thiols to inhibit or alter protein activity (25).…”

mentioning

confidence: 99%

Fe(II) Oxidation Is an Innate Capability of Nitrate-Reducing Bacteria That Involves Abiotic and Biotic Reactions

Carlson

Clark²,

Blazewicz³

et al. 2013

Journal of Bacteriology

153

160

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Phylogenetically diverse species of bacteria can catalyze the oxidation of ferrous iron [Fe(II)] coupled to nitrate (NO 3؊ ) reduction, often referred to as nitrate-dependent iron oxidation (NDFO). Very little is known about the biochemistry of NDFO, and though growth benefits have been observed, mineral encrustations and nitrite accumulation likely limit growth. Acidovorax ebreus, like other species in the Acidovorax genus, is proficient at catalyzing NDFO. Our results suggest that the induction of specific Fe(II) oxidoreductase proteins is not required for NDFO. No upregulated periplasmic or outer membrane redox-active proteins, like those involved in Fe(II) oxidation by acidophilic iron oxidizers or anaerobic photoferrotrophs, were observed in proteomic experiments. We demonstrate that while "abiotic" extracellular reactions between Fe(II) and biogenic NO 2 ؊ /NO can be involved in NDFO, intracellular reactions between Fe(II) and periplasmic components are essential to initiate extensive NDFO. We present evidence that an organic cosubstrate inhibits NDFO, likely by keeping periplasmic enzymes in their reduced state, stimulating metal efflux pumping, or both, and that growth during NDFO relies on the capacity of a nitrate-reducing bacterium to overcome the toxicity of Fe(II) and reactive nitrogen species. On the basis of our data and evidence in the literature, we postulate that all respiratory nitrate-reducing bacteria are innately capable of catalyzing NDFO. Our findings have implications for a mechanistic understanding of NDFO, the biogeochemical controls on anaerobic Fe(II) oxidation, and the production of NO 2 ؊ , NO, and N 2 O in the environment.

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Complex Formation between Metallic Cations and Proteins, Peptides, and Amino Acids

Cited by 322 publications

References 246 publications

Observations on the Mechanism of Copper Damage in Chlorella

Observations on the Mechanism of Copper Damage in Chlorella

Etude cristallographique du perchlorate de dihistamino-cuivre(II)

Fe(II) Oxidation Is an Innate Capability of Nitrate-Reducing Bacteria That Involves Abiotic and Biotic Reactions

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