A structural and functional model for dioxygenases with a 2-His-1-carboxylate triad

Paul D. Oldenburg; Chun Yen Ke; A. Alex Tipton; Albert A. Shteinman; Larry Que

doi:10.1002/anie.200603486

A structural and functional model for dioxygenases with a 2-His-1-carboxylate triad

Paul D. Oldenburg
, Chun Yen Ke
, A. Alex Tipton
, Albert A. Shteinman
, Larry Que

Chemistry (Twin Cities)

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

58 Scopus citations

Abstract

(Chemical Equation Presented) An attractive model: The iron complex shown on the left models the 2-His-1-carboxylate active sites of Rieske dioxygenases both in terms of structure and function. ¹⁸O-labeling studies of olefin dihydroxylation support the involvement of a high-valent iron-oxo species.

Original language	English (US)
Pages (from-to)	7975-7978
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	45
Issue number	47
DOIs	https://doi.org/10.1002/anie.200603486
State	Published - Dec 4 2006

Keywords

Dihydroxylation
Dioxygenases
Enzyme models
Epoxidation
Oxidation

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10.1002/anie.200603486

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abstract = "(Chemical Equation Presented) An attractive model: The iron complex shown on the left models the 2-His-1-carboxylate active sites of Rieske dioxygenases both in terms of structure and function. 18O-labeling studies of olefin dihydroxylation support the involvement of a high-valent iron-oxo species.",

keywords = "Dihydroxylation, Dioxygenases, Enzyme models, Epoxidation, Oxidation",

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AU - Oldenburg, Paul D.

AU - Ke, Chun Yen

AU - Tipton, A. Alex

AU - Shteinman, Albert A.

AU - Que, Larry

PY - 2006/12/4

Y1 - 2006/12/4

N2 - (Chemical Equation Presented) An attractive model: The iron complex shown on the left models the 2-His-1-carboxylate active sites of Rieske dioxygenases both in terms of structure and function. 18O-labeling studies of olefin dihydroxylation support the involvement of a high-valent iron-oxo species.

AB - (Chemical Equation Presented) An attractive model: The iron complex shown on the left models the 2-His-1-carboxylate active sites of Rieske dioxygenases both in terms of structure and function. 18O-labeling studies of olefin dihydroxylation support the involvement of a high-valent iron-oxo species.

KW - Dihydroxylation

KW - Dioxygenases

KW - Enzyme models

KW - Epoxidation

KW - Oxidation

UR - https://www.scopus.com/pages/publications/33845480978

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U2 - 10.1002/anie.200603486

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AN - SCOPUS:33845480978

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 47

ER -

A structural and functional model for dioxygenases with a 2-His-1-carboxylate triad

Abstract

Keywords

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