Biomimetic Thiolate Alkylation with Zinc Pyrazolylbis(thioimidazolyl)borate Complexes

Biomimetic Thiolate Alkylation with Zinc Pyrazolylbis(thioimidazolyl)borate Complexes

The NS2ZnX coordination in thiolate‐alkylating zinc enzymes is reproduced in (tripod)ZnX complexes with substituted pyrazolylbis(thioimidazolyl)borate tripod ligands. Intermediate (tripod)Zn nitrates and perchlorates are converted into (tripod)Zn thiolates, including the biologically relevant homocy...

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Veröffentlicht in:European Journal of Inorganic Chemistry 2005-10, Vol.2005 (20), p.4070-4077
Hauptverfasser: Ibrahim, Mohamed M., He, Guosen, Seebacher, Jan, Benkmil, Boumahdi, Vahrenkamp, Heinrich
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Bioinorganic chemistry
Enzyme models
N,S ligands
S ligands
Thiolates
Zinc
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container_end_page 4077
container_issue 20
container_start_page 4070
container_title European Journal of Inorganic Chemistry
container_volume 2005
creator Ibrahim, Mohamed M.
He, Guosen
Seebacher, Jan
Benkmil, Boumahdi
Vahrenkamp, Heinrich
description The NS2ZnX coordination in thiolate‐alkylating zinc enzymes is reproduced in (tripod)ZnX complexes with substituted pyrazolylbis(thioimidazolyl)borate tripod ligands. Intermediate (tripod)Zn nitrates and perchlorates are converted into (tripod)Zn thiolates, including the biologically relevant homocysteinate. Methylation with CH3I converts these to (tripod)ZnI and the corresponding thioethers CH3SR, including methionine. A kinetic investigation has shown the alkylations to be intramolecular SN2 processes that take place at the zinc‐bound thiolates. They are considerably faster for the (NS2)Zn thiolates than for the (N2S)‐ and (N3)Zn‐thiolates with similar pyrazolylborate‐derived tripod ligands, in agreement with Nature’s choice of an NS2 donor set for zinc. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)
doi_str_mv 10.1002/ejic.200500276
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subjects Bioinorganic chemistry
Enzyme models
N,S ligands
S ligands
Thiolates
Zinc
title Biomimetic Thiolate Alkylation with Zinc Pyrazolylbis(thioimidazolyl)borate Complexes
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