New synthetic models of cytochrome P450: How different are they from the natural species?

Sebastian Kozuch; Tycho Leifels; Dominik Meyer; Laura Sbaragli; Sason Shaik; Wolf D. Woggon

doi:10.1055/s-2005-863724

New synthetic models of cytochrome P450: How different are they from the natural species?

Sebastian Kozuch
, Tycho Leifels
, Dominik Meyer
, Laura Sbaragli
, Sason Shaik
, Wolf D. Woggon

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

21 Scopus citations

Abstract

Soluble and matrix-bound P450 enzyme models have been synthesized carrying a SO₃^- ligand coordinating to iron. These complexes display features very similar to cofactors of enzymes such as P450_cam with respect to electrochemistry and UV/Vis spectroscopy. Further they catalyze epoxidation reactions with turnover numbers up to 1800. DFT calculations revealed that the coordination of SO₃^- to Fe(III) produces an active species that displays allylic hydroxylation and epoxidation reactivity patterns that are nearly indistinguishable from those calculated for the natural active species of the enzyme cytochrome P450.

Original language	English
Pages (from-to)	675-684
Number of pages	10
Journal	Synlett
Issue number	4
DOIs	https://doi.org/10.1055/s-2005-863724
State	Published - 4 Mar 2005
Externally published	Yes

Keywords

Catalysis
DFT calculations
Enzyme models
Hemethiolate proteins
Iron porphyrins

ASJC Scopus subject areas

Organic Chemistry

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10.1055/s-2005-863724

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title = "New synthetic models of cytochrome P450: How different are they from the natural species?",

abstract = "Soluble and matrix-bound P450 enzyme models have been synthesized carrying a SO3- ligand coordinating to iron. These complexes display features very similar to cofactors of enzymes such as P450cam with respect to electrochemistry and UV/Vis spectroscopy. Further they catalyze epoxidation reactions with turnover numbers up to 1800. DFT calculations revealed that the coordination of SO3- to Fe(III) produces an active species that displays allylic hydroxylation and epoxidation reactivity patterns that are nearly indistinguishable from those calculated for the natural active species of the enzyme cytochrome P450.",

keywords = "Catalysis, DFT calculations, Enzyme models, Hemethiolate proteins, Iron porphyrins",

author = "Sebastian Kozuch and Tycho Leifels and Dominik Meyer and Laura Sbaragli and Sason Shaik and Woggon, \{Wolf D.\}",

year = "2005",

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doi = "10.1055/s-2005-863724",

language = "English",

pages = "675--684",

journal = "Synlett",

issn = "0936-5214",

publisher = "Georg Thieme Verlag",

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T1 - New synthetic models of cytochrome P450

T2 - How different are they from the natural species?

AU - Kozuch, Sebastian

AU - Leifels, Tycho

AU - Meyer, Dominik

AU - Sbaragli, Laura

AU - Shaik, Sason

AU - Woggon, Wolf D.

PY - 2005/3/4

Y1 - 2005/3/4

N2 - Soluble and matrix-bound P450 enzyme models have been synthesized carrying a SO3- ligand coordinating to iron. These complexes display features very similar to cofactors of enzymes such as P450cam with respect to electrochemistry and UV/Vis spectroscopy. Further they catalyze epoxidation reactions with turnover numbers up to 1800. DFT calculations revealed that the coordination of SO3- to Fe(III) produces an active species that displays allylic hydroxylation and epoxidation reactivity patterns that are nearly indistinguishable from those calculated for the natural active species of the enzyme cytochrome P450.

AB - Soluble and matrix-bound P450 enzyme models have been synthesized carrying a SO3- ligand coordinating to iron. These complexes display features very similar to cofactors of enzymes such as P450cam with respect to electrochemistry and UV/Vis spectroscopy. Further they catalyze epoxidation reactions with turnover numbers up to 1800. DFT calculations revealed that the coordination of SO3- to Fe(III) produces an active species that displays allylic hydroxylation and epoxidation reactivity patterns that are nearly indistinguishable from those calculated for the natural active species of the enzyme cytochrome P450.

KW - Catalysis

KW - DFT calculations

KW - Enzyme models

KW - Hemethiolate proteins

KW - Iron porphyrins

UR - https://www.scopus.com/pages/publications/15444379907

U2 - 10.1055/s-2005-863724

DO - 10.1055/s-2005-863724

M3 - Article

AN - SCOPUS:15444379907

SN - 0936-5214

SP - 675

EP - 684

JO - Synlett

JF - Synlett

IS - 4

ER -

New synthetic models of cytochrome P450: How different are they from the natural species?

Abstract

Keywords

ASJC Scopus subject areas

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