Iron complexes with an N/S chromophore relevant to the active site of the hydrolytic metalloenzyme nitrile hydratase

Nivorozhkin Alexandre; Uraev Ali; Bondarenko Gennadii; Antsyshkina Alla; Kurbatov Vasilii; Garnovskii Alexander; Turta Constantin; Brashoveanu Nikolai

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131

SM ISO690:2012

NIVOROZHKIN, Alexandre, URAEV, Ali, BONDARENKO, Gennadii, ANTSYSHKINA, Alla, KURBATOV, Vasilii, GARNOVSKII, Alexander, TURTA, Constantin, BRASHOVEANU, Nikolai. Iron complexes with an N/S chromophore relevant to the active site of the hydrolytic metalloenzyme nitrile hydratase. In: Chemical Communications, 1997, pp. 1711-1712. ISSN 1359-7345. DOI: https://doi.org/10.1039/a704879c

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Chemical Communications

/ 1997 / ISSN 1359-7345 /ISSNe 1364-548X

Iron complexes with an N/S chromophore relevant to the active site of the hydrolytic metalloenzyme nitrile hydratase

DOI:https://doi.org/10.1039/a704879c

Pag. 1711-1712

Nivorozhkin Alexandre¹², Uraev Ali¹, Bondarenko Gennadii¹, Antsyshkina Alla³, Kurbatov Vasilii¹, Garnovskii Alexander¹, Turta Constantin⁴, Brashoveanu Nikolai⁴

¹ Rostov State University,
² Harvard University,
³ Kurnakov Institute of General and Inorganic Chemistry of the RAS, Moscow ,
⁴ Institute of Chemistry of the Academy of Sciences of Moldova

Disponibil în IBN: 17 iulie 2023

Rezumat

Iron(III) complexes with a 3N/3S chromophore reproduce a mixed N/S heterocyclic ligand environment, metal-ligand bond lengths, and low-spin state (S = 1/2) characteristic of the hydrolytic metalloenzyme nitrile hydratase; Fe^IIIN₂S₂Cl species possesses a quantum mechanically admixed S = 3/2, 5/2 state and able to form low-spin solvent adducts, possible analogues of the substrate-bound form of the enzyme.