Synthesis and characterization of dinuclear complexes containing the FeIII–F  · · ·  (H2O)MII motif

Ghiladi, Morten; Jensen, Kenneth; Jiang, Jianzhong; McKenzie, Christine J.; Mørup, Steen; Søtofte, Inger; Ulstrup, Jens

doi:10.1039/a902678i

Cited by 40 publications

(32 citation statements)

References 34 publications

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“…4) shows that the ligand is coordinated to the Ni(II) center in a facial mode and meridionally to the Fe(III). There is no acetate bridge and the metal ions are bound only to the phenoxo bridge from the bpbpmp 2- [51,52].…”

Section: Kinetic Properties Of Fe(iii)ni(ii)-ufmentioning

confidence: 99%

Probing the role of the divalent metal ion in uteroferrin using metal ion replacement and a comparison to isostructural biomimetics

et al. 2007

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Purple acid phosphatases (PAPs) are a group of heterovalent binuclear metalloenzymes that catalyze the hydrolysis of phosphomonoesters at acidic to neutral pH. While the metal ions are essential for catalysis, their precise roles are not fully understood. Here, the Fe(III)Ni(II) derivative of pig PAP (uteroferrin) was generated and its properties were compared with those of the native Fe(III)Fe(II) enzyme. The k cat of the Fe(III)Ni(II) derivative (approximately 60 s -1 ) is approximately 20% of that of native uteroferrin, and the Ni(II) uptake is considerably faster than the reconstitution of full enzymatic activity, suggesting a slow conformational change is required to attain optimal reactivity. An analysis of the pH dependence of the catalytic properties of Fe(III)Ni(II) uteroferrin indicates that the l-hydroxide is the likely nucleophile. Thus, the Ni(II) derivative employs a mechanism similar to that proposed for the Ga(III)Zn(II) derivative of uteroferrin, but different from that of the native enzyme, which uses a terminal Fe(III)-bound nucleophile to initiate catalysis. Binuclear Fe(III)Ni(II) biomimetics with coordination environments similar to the coordination environment of uteroferrin were generated to provide both experimental benchmarks (structural and spectroscopic) and further insight into the catalytic mechanism of hydrolysis. The data are consistent with a reaction mechanism employing an Fe(III)-bound terminal hydroxide as a nucleophile, similar to that proposed for native uteroferrin and various related isostructural biomimetics. Thus, only in the uteroferrin-catalyzed reaction are the precise details of the catalytic mechanism sensitive to the metal ion composition, illustrating the significance of the dynamic ligand environment in the protein active site for the optimization of the catalytic efficiency.

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Section: Kinetic Properties Of Fe(iii)ni(ii)-ufmentioning

confidence: 99%

Probing the role of the divalent metal ion in uteroferrin using metal ion replacement and a comparison to isostructural biomimetics

et al. 2007

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“…Furthermore, it is quite unique that the differences between the redox potential values of Fe II Fe III /Fe III Fe III and Fe II Fe II /Fe II Fe III couples for 1-4, DE, are very close in comparison with those of diiron complexes reported hitherto[30,35,[40][41][42][43][44][45]. The smaller DE values in complexes 1-4 must have been induced by the protonation/deprotonation of the OH group of HTPPDO.…”

mentioning

confidence: 55%

Diiron(II) complexes showing a reversible oxygenation induced by a proton transfer mediated with a water molecule. Biological implication of a water molecule in hemerythrin function

Arii

Funahashi

Ozawa

et al. 2007

Journal of Organometallic Chemistry

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“…The data obtained by CPE indicate that the electrochemical behaviour of the coordination polymers is driven by the characteristics of the substituent at the camphor ligand (Y) in contrast to the redox potentials (CV). An electron count less than two (1a and 1b) suggests that upon one electron oxidation the rupture of the chain -Cu-Cl-Cu-Cl-occurs, forming CuCl 2 plus a copper species ({CuL} + ) that does not oxidize at the potential of CPE (1b) or further reacts (1a [7,8]. Further evidence for [CuL] + comes from the IR spectra that display a considerable shift to higher values of ν CO (1762 cm −1 ) and ν CN (1663 cm −1 ) compared to the corresponding in 1a (ν CO =1691; ν CN =1550 cm −1 ).…”

Section: Cpe Studiesmentioning

confidence: 99%

Redox Properties of CU(I) Camphor Hydrazone Complexes

Fernanda

Carvalho²,

Fernandes³

2011

Port. Electrochim. Acta

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The electrochemical properties of the one-dimensional coordination polymers [{CuX} 2 (YNC 10 H 14 O)] n (X=Cl: Y=NMe 2 1a, Y=NHMe 1b, Y=NH 2 1c; X=Br: Y=NH 2 2c) and dimers [{Cu(YNC 10 H 14 O)} 2 (µ-X) 2 ] (X=Cl: Y=NMe 2 3a; Y=NHMe 3b; X=Br: Y=NMe 2 4a; Y=NHMe 4b) were studied by cyclic voltammetry (CV) and controlled potential electrolysis (CPE). All complexes display anodic and cathodic processes. The anodic processes involve the oxidation of the metal site (Cu(I) Cu(II)), while the cathodic processes are based on the ligand. The substituent (Y) at the camphor hydrazones (YNC 10 H 14 O) plays a relevant role in the electrochemical properties and reactivity of Cu(I) coordination polymers and Cu(I) dimmers, as corroborated by CPE.

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Synthesis and characterization of dinuclear complexes containing the FeIII–F · · · (H2O)MII motif

Cited by 40 publications

References 34 publications

Probing the role of the divalent metal ion in uteroferrin using metal ion replacement and a comparison to isostructural biomimetics

Probing the role of the divalent metal ion in uteroferrin using metal ion replacement and a comparison to isostructural biomimetics

Diiron(II) complexes showing a reversible oxygenation induced by a proton transfer mediated with a water molecule. Biological implication of a water molecule in hemerythrin function

Redox Properties of CU(I) Camphor Hydrazone Complexes

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