Insights into the role of zinc(II) sites in hydrolytic enzymes: Study of the ZnII/X/(py)2CO (X = Cl-, N3-, SO42-; (py)2CO=di-2-pyridyl ketone) reaction systems

Kenichi Nishioka; Judd C. Rice; Kavitha Sarma; Hediye Erdjument-Bromage; Janis Werner; Yanming Wang; Sergei Chuikov; Pablo Valenzuela; Paul Tempst; Ruth Steward; John T. Lis; C. David Allis; Danny Reinberg

doi:10.1016/S1387-7003(02)00542-7

Insights into the role of zinc(II) sites in hydrolytic enzymes: Study of the Zn^II/X/(py)₂CO (X = Cl^-, N₃^-, SO₄^2-; (py)₂CO=di-2-pyridyl ketone) reaction systems

Kenichi Nishioka, Judd C. Rice, Kavitha Sarma, Hediye Erdjument-Bromage, Janis Werner, Yanming Wang, Sergei Chuikov, Pablo Valenzuela, Paul Tempst, Ruth Steward, John T. Lis, C. David Allis, Danny Reinberg

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

Abstract

A bioinorganic model approach for the investigation of substrate activation by zinc active sites in hydrolytic enzymes has been initiated. Several reaction schemes involving the substrate analogue di-2-pyridyl ketone, (py)₂CO, and Zn(II) sources afforded the new complexes [ZnCl₂{(py)₂CO}](1), [ZnCl₂{(py)₂C(OMe)(OH)}](2), [Zn₂Cl₂{(py)₂C(OMe)O}₂](3), [Zn₂(N₃)₂{(py)₂C(OMe) O}₂](4) and [Zn₂(SO₄)₂{(py)₂C(OMe) (OH)}₂(MeOH)₂](5), which have been characterized by single-crystal X-ray crystallography and spectroscopic techniques. The chemical and structural identity of the products depends on the solvent, the hydroxide concentration and the nature of the inorganic anion. The biological relevance of the prepared complexes is also discussed.

Original language	English (US)
Pages (from-to)	719-723
Number of pages	5
Journal	Inorganic Chemistry Communications
Volume	5
Issue number	9
DOIs	https://doi.org/10.1016/S1387-7003(02)00542-7
State	Published - Sep 1 2002

All Science Journal Classification (ASJC) codes

Physical and Theoretical Chemistry
Inorganic Chemistry
Materials Chemistry

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Nishioka, K., Rice, J. C., Sarma, K., Erdjument-Bromage, H., Werner, J., Wang, Y., Chuikov, S., Valenzuela, P., Tempst, P., Steward, R., Lis, J. T., Allis, C. D., & Reinberg, D. (2002). Insights into the role of zinc(II) sites in hydrolytic enzymes: Study of the Zn^II/X/(py)₂CO (X = Cl^-, N₃^-, SO₄^2-; (py)₂CO=di-2-pyridyl ketone) reaction systems. Inorganic Chemistry Communications, 5(9), 719-723. https://doi.org/10.1016/S1387-7003(02)00542-7

Nishioka, Kenichi ; Rice, Judd C. ; Sarma, Kavitha ; Erdjument-Bromage, Hediye ; Werner, Janis ; Wang, Yanming ; Chuikov, Sergei ; Valenzuela, Pablo ; Tempst, Paul ; Steward, Ruth ; Lis, John T. ; Allis, C. David ; Reinberg, Danny. / Insights into the role of zinc(II) sites in hydrolytic enzymes : Study of the Zn^II/X/(py)₂CO (X = Cl^-, N₃^-, SO₄^2-; (py)₂CO=di-2-pyridyl ketone) reaction systems. In: Inorganic Chemistry Communications. 2002 ; Vol. 5, No. 9. pp. 719-723.

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title = "Insights into the role of zinc(II) sites in hydrolytic enzymes: Study of the ZnII/X/(py)2CO (X = Cl-, N3-, SO42-; (py)2CO=di-2-pyridyl ketone) reaction systems",

abstract = "A bioinorganic model approach for the investigation of substrate activation by zinc active sites in hydrolytic enzymes has been initiated. Several reaction schemes involving the substrate analogue di-2-pyridyl ketone, (py)2CO, and Zn(II) sources afforded the new complexes [ZnCl2{(py)2CO}](1), [ZnCl2{(py)2C(OMe)(OH)}](2), [Zn2Cl2{(py)2C(OMe)O}2](3), [Zn2(N3)2{(py)2C(OMe) O}2](4) and [Zn2(SO4)2{(py)2C(OMe) (OH)}2(MeOH)2](5), which have been characterized by single-crystal X-ray crystallography and spectroscopic techniques. The chemical and structural identity of the products depends on the solvent, the hydroxide concentration and the nature of the inorganic anion. The biological relevance of the prepared complexes is also discussed.",

author = "Kenichi Nishioka and Rice, {Judd C.} and Kavitha Sarma and Hediye Erdjument-Bromage and Janis Werner and Yanming Wang and Sergei Chuikov and Pablo Valenzuela and Paul Tempst and Ruth Steward and Lis, {John T.} and Allis, {C. David} and Danny Reinberg",

year = "2002",

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doi = "10.1016/S1387-7003(02)00542-7",

language = "English (US)",

volume = "5",

pages = "719--723",

journal = "Inorganic Chemistry Communication",

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Nishioka, K, Rice, JC, Sarma, K, Erdjument-Bromage, H, Werner, J, Wang, Y, Chuikov, S, Valenzuela, P, Tempst, P, Steward, R, Lis, JT, Allis, CD & Reinberg, D 2002, 'Insights into the role of zinc(II) sites in hydrolytic enzymes: Study of the Zn^II/X/(py)₂CO (X = Cl^-, N₃^-, SO₄^2-; (py)₂CO=di-2-pyridyl ketone) reaction systems', Inorganic Chemistry Communications, vol. 5, no. 9, pp. 719-723. https://doi.org/10.1016/S1387-7003(02)00542-7

Insights into the role of zinc(II) sites in hydrolytic enzymes : Study of the Zn^II/X/(py)₂CO (X = Cl^-, N₃^-, SO₄^2-; (py)₂CO=di-2-pyridyl ketone) reaction systems. / Nishioka, Kenichi; Rice, Judd C.; Sarma, Kavitha; Erdjument-Bromage, Hediye; Werner, Janis; Wang, Yanming; Chuikov, Sergei; Valenzuela, Pablo; Tempst, Paul; Steward, Ruth; Lis, John T.; Allis, C. David; Reinberg, Danny.

In: Inorganic Chemistry Communications, Vol. 5, No. 9, 01.09.2002, p. 719-723.

Research output: Contribution to journal › Article › peer-review

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T2 - Study of the ZnII/X/(py)2CO (X = Cl-, N3-, SO42-; (py)2CO=di-2-pyridyl ketone) reaction systems

AU - Nishioka, Kenichi

AU - Rice, Judd C.

AU - Sarma, Kavitha

AU - Erdjument-Bromage, Hediye

AU - Werner, Janis

AU - Wang, Yanming

AU - Chuikov, Sergei

AU - Valenzuela, Pablo

AU - Tempst, Paul

AU - Steward, Ruth

AU - Lis, John T.

AU - Allis, C. David

AU - Reinberg, Danny

PY - 2002/9/1

Y1 - 2002/9/1

N2 - A bioinorganic model approach for the investigation of substrate activation by zinc active sites in hydrolytic enzymes has been initiated. Several reaction schemes involving the substrate analogue di-2-pyridyl ketone, (py)2CO, and Zn(II) sources afforded the new complexes [ZnCl2{(py)2CO}](1), [ZnCl2{(py)2C(OMe)(OH)}](2), [Zn2Cl2{(py)2C(OMe)O}2](3), [Zn2(N3)2{(py)2C(OMe) O}2](4) and [Zn2(SO4)2{(py)2C(OMe) (OH)}2(MeOH)2](5), which have been characterized by single-crystal X-ray crystallography and spectroscopic techniques. The chemical and structural identity of the products depends on the solvent, the hydroxide concentration and the nature of the inorganic anion. The biological relevance of the prepared complexes is also discussed.

AB - A bioinorganic model approach for the investigation of substrate activation by zinc active sites in hydrolytic enzymes has been initiated. Several reaction schemes involving the substrate analogue di-2-pyridyl ketone, (py)2CO, and Zn(II) sources afforded the new complexes [ZnCl2{(py)2CO}](1), [ZnCl2{(py)2C(OMe)(OH)}](2), [Zn2Cl2{(py)2C(OMe)O}2](3), [Zn2(N3)2{(py)2C(OMe) O}2](4) and [Zn2(SO4)2{(py)2C(OMe) (OH)}2(MeOH)2](5), which have been characterized by single-crystal X-ray crystallography and spectroscopic techniques. The chemical and structural identity of the products depends on the solvent, the hydroxide concentration and the nature of the inorganic anion. The biological relevance of the prepared complexes is also discussed.

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DO - 10.1016/S1387-7003(02)00542-7

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EP - 723

JO - Inorganic Chemistry Communication

JF - Inorganic Chemistry Communication

SN - 1387-7003

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