Zinc enzyme modelling with zinc complexes of polar pyrazolylborate ligands

Olmo, Cristina Pérez; Böhmerle, Karin; Vahrenkamp, Heinrich

doi:10.1016/j.ica.2006.08.021

Cited by 16 publications

(5 citation statements)

References 31 publications

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“…In solution ligands L 1 and L 2 form zinc-aqua complexes which are stable in DMSO-water or methanol-water solutions containing the MOPS buffer. 47 In these solutions they catalyze the hydrolysis of p-nitrophenyl acetate and tris(p-nitrophenyl)phosphate (TNP). The best catalyst is that with L 2 which is able to remove two p-nitrophenyl groups from TNP.…”

Section: Last But Not Least: Catalytic Tp*zn Chemistrymentioning

confidence: 99%

Why does nature use zinc-a personal view

Vahrenkamp

2007

Dalton Trans.

145

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In this perspective some results from the work by the author's research group on the coordination chemistry of zinc are presented. They are selected so as to highlight the principles which, in the opinion of the author, make zinc unique in its ability to function as the catalytic center for an ever-increasing number of biological processes. In essence, the "non-properties" of zinc are the basis of its success: no redox chemistry, no ligand field effects, no typical coordination numbers or geometries, no stability or inertness of its complexes, no typical "hard" or "soft" characteristics. The chemistry presented here is centered around the "Freiburg Enzyme Model", the pyrazolylborate-ligated zinc-hydroxide complex. The topics discussed in detail include the zinc-water combination, the non-similarity between the Zn-OH and the Zn-SH, Zn-OR or Zn-SR complexes, and the functionalization of CO(2) by zinc-bound nucleophiles. The value of structure correlation analysis for the elucidation of mechanistic details is demonstrated, and the first examples of catalysis by the TpZn-OH complexes are presented.

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Section: Last But Not Least: Catalytic Tp*zn Chemistrymentioning

confidence: 99%

Why does nature use zinc-a personal view

Vahrenkamp

2007

Dalton Trans.

145

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“…Nevertheless, the experienced coordination chemist can advance the field by proposing new ligand types for enzyme inhibitors, as we believe to have done in this and the preceding paper . Furthermore, we have started a new generation of Tp ligands with hydrogen-bonding substituents. , As our activities in the field of biomimetic zinc chemistry have come to an end, it is only left to us to express our optimism that our successors will continue making significant contributions to this area of the life sciences from the field of inorganic chemistry.…”

Section: Discussionmentioning

confidence: 84%

“…29 Furthermore, we have started a new generation of Tp ligands with hydrogen-bonding substituents. 46,47 As our activities in the field of biomimetic zinc chemistry have come to an end, it is only left to us to express our optimism that our successors will continue making significant contributions to this area of the life sciences from the field of inorganic chemistry.…”

Section: Discussionmentioning

confidence: 99%

Modeling Zinc Enzyme Inhibition with Functional Thiolate Ligands

Tekeste

Vahrenkamp

2006

Inorg. Chem.

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The blocking of zinc enzymes by thiolate-containing inhibitors was modeled by treating TpPh,MeZn-OH with functional thiols. The latter were chosen such that they contain an additional donor function (COOH, COOR, NH2, NHR, OH) in a position favorable for chelation. Of them, mercapto carboxylic acid esters were incorporated as thiolates. The corresponding mercapto carboxylic acids, however, used only their carboxylate function for coordination. Various mercapto amines, mercapto alcohols, and mercaptophenol were exclusively converted to thiolate ligands. The two modes of inhibitor attachment, terminal or chelating, were observed equally frequently. As a rule, they occur as alternatives for similar ligands. In case of 2-mercaptophenol they coexist in the crystalline state and in solution. Hydrogen bonding, both intra- and intermolecular, seems to be a decisive factor determining the inhibitor attachments. Its persistence in solution is underlined by the observation that TpPh,MeZn-hydroxythiophenolates are methylated about 2 orders of magnitude slower than TpPh,MeZn-SPh itself.

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“…185 The crystallographic characterisation of six states of blasticidin S and blasticidin S deaminase have shown that the zinc centre, which is coordinated by three cysteine and one water ligand, moves considerably during the catalytic cycle, probably due to the steric requirement of the substrate during the reaction. 186 Water-soluble tris(pyrazolyl)borate 187 and tris(triazolyl)borate 188 ligands and their zinc complexes have been prepared. The former are the first to show catalytic activity in biomimetic hydrolysis reactions.…”

Section: Zincmentioning

confidence: 99%

Bioinorganic chemistry

Duhme‐Klair

2008

Annu. Rep. Prog. Chem., Sect. A: Inorg. Chem.

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Zinc enzyme modelling with zinc complexes of polar pyrazolylborate ligands

Cited by 16 publications

References 31 publications

Why does nature use zinc-a personal view

Why does nature use zinc-a personal view

Modeling Zinc Enzyme Inhibition with Functional Thiolate Ligands

Bioinorganic chemistry

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