Geometry-Dependent Phosphodiester Hydrolysis Catalyzed by Binuclear Copper Complexes

Lei Zhu; Osvaldo Dos Santos; Chi Wan Koo; Marc Rybstein; Louise Pape; James W. Canary

doi:10.1021/ic0340985

Geometry-Dependent Phosphodiester Hydrolysis Catalyzed by Binuclear Copper Complexes

Lei Zhu, Osvaldo Dos Santos, Chi Wan Koo, Marc Rybstein, Louise Pape, James W. Canary

Radiology

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Abstract

Two isomeric binuclear ligands PBTPA and MBTPA and their copper(II) complexes were prepared and examined for hydrolysis of a model phosphodiester substrate: bis(p-nitrophenyl) phosphate. A bell-shaped pH vs rate profile, which is in agreement with one mechanism proposed for bimetallonucleases/phosphatases, was observed for the binuclear complex of copper(II) and PBTPA. At pH 8.4, a maximum rate of 1.14 × 10^-6 s^-1-more than 10⁴-fold over uncatalyzed reactions-was achieved. However, the analogous complex of MBTPA did not show significant rate enhancement. The binuclear complex of copper(II) and PBTPA also showed 10-fold acceleration over mononuclear complex of copper(II) and tris(2-pyridylmethyl)amine (TPA) catalyzed reaction. A phage φX174 DNA assay showed that the complex of copper(II) and PBTPA promoted supercoiled phage φX174 DNA relaxation under both aerobic and anaerobic conditions, in contrast to the hydrolytic inactivity of the mononuclear complex of copper(II) and TPA.

Original language	English (US)
Pages (from-to)	7912-7920
Number of pages	9
Journal	Inorganic Chemistry
Volume	42
Issue number	24
DOIs	https://doi.org/10.1021/ic0340985
State	Published - Dec 1 2003

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry

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title = "Geometry-Dependent Phosphodiester Hydrolysis Catalyzed by Binuclear Copper Complexes",

abstract = "Two isomeric binuclear ligands PBTPA and MBTPA and their copper(II) complexes were prepared and examined for hydrolysis of a model phosphodiester substrate: bis(p-nitrophenyl) phosphate. A bell-shaped pH vs rate profile, which is in agreement with one mechanism proposed for bimetallonucleases/phosphatases, was observed for the binuclear complex of copper(II) and PBTPA. At pH 8.4, a maximum rate of 1.14 × 10-6 s-1-more than 104-fold over uncatalyzed reactions-was achieved. However, the analogous complex of MBTPA did not show significant rate enhancement. The binuclear complex of copper(II) and PBTPA also showed 10-fold acceleration over mononuclear complex of copper(II) and tris(2-pyridylmethyl)amine (TPA) catalyzed reaction. A phage φX174 DNA assay showed that the complex of copper(II) and PBTPA promoted supercoiled phage φX174 DNA relaxation under both aerobic and anaerobic conditions, in contrast to the hydrolytic inactivity of the mononuclear complex of copper(II) and TPA.",

author = "Lei Zhu and {Dos Santos}, Osvaldo and Koo, {Chi Wan} and Marc Rybstein and Louise Pape and Canary, {James W.}",

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AU - Zhu, Lei

AU - Dos Santos, Osvaldo

AU - Koo, Chi Wan

AU - Rybstein, Marc

AU - Pape, Louise

AU - Canary, James W.

PY - 2003/12/1

Y1 - 2003/12/1

N2 - Two isomeric binuclear ligands PBTPA and MBTPA and their copper(II) complexes were prepared and examined for hydrolysis of a model phosphodiester substrate: bis(p-nitrophenyl) phosphate. A bell-shaped pH vs rate profile, which is in agreement with one mechanism proposed for bimetallonucleases/phosphatases, was observed for the binuclear complex of copper(II) and PBTPA. At pH 8.4, a maximum rate of 1.14 × 10-6 s-1-more than 104-fold over uncatalyzed reactions-was achieved. However, the analogous complex of MBTPA did not show significant rate enhancement. The binuclear complex of copper(II) and PBTPA also showed 10-fold acceleration over mononuclear complex of copper(II) and tris(2-pyridylmethyl)amine (TPA) catalyzed reaction. A phage φX174 DNA assay showed that the complex of copper(II) and PBTPA promoted supercoiled phage φX174 DNA relaxation under both aerobic and anaerobic conditions, in contrast to the hydrolytic inactivity of the mononuclear complex of copper(II) and TPA.

AB - Two isomeric binuclear ligands PBTPA and MBTPA and their copper(II) complexes were prepared and examined for hydrolysis of a model phosphodiester substrate: bis(p-nitrophenyl) phosphate. A bell-shaped pH vs rate profile, which is in agreement with one mechanism proposed for bimetallonucleases/phosphatases, was observed for the binuclear complex of copper(II) and PBTPA. At pH 8.4, a maximum rate of 1.14 × 10-6 s-1-more than 104-fold over uncatalyzed reactions-was achieved. However, the analogous complex of MBTPA did not show significant rate enhancement. The binuclear complex of copper(II) and PBTPA also showed 10-fold acceleration over mononuclear complex of copper(II) and tris(2-pyridylmethyl)amine (TPA) catalyzed reaction. A phage φX174 DNA assay showed that the complex of copper(II) and PBTPA promoted supercoiled phage φX174 DNA relaxation under both aerobic and anaerobic conditions, in contrast to the hydrolytic inactivity of the mononuclear complex of copper(II) and TPA.

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Geometry-Dependent Phosphodiester Hydrolysis Catalyzed by Binuclear Copper Complexes

Abstract

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