Computer-generated high-valent iron-oxo and manganese-oxo species with polyoxometalate ligands: How do they compare with the iron-oxo active species of heme enzymes?

Samüel P. De Visser, Devesh Kumar, Ronny Neumann, Sason Shaik

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

The structure and reactivity of high-valent FeVO and Mn VIO oxidation catalysts containing a polyoxometalate [PW 11O39]7- lacunary ligand (2) have been investigated by a computational study. Calculations have demonstrated there is an intriguing analogy between these species and the active species (1) of the enzyme cytochrome P450 (see scheme).

Original languageEnglish
Pages (from-to)5661-5665
Number of pages5
JournalAngewandte Chemie - International Edition
Volume43
Issue number42
DOIs
Publication statusPublished - Oct 25 2004

Fingerprint

Manganese
Heme
Cytochrome P-450 Enzyme System
Iron
Enzymes
Ligands
Oxidation
Catalysts
polyoxometalate I

Keywords

  • Cytochrome P450
  • Density functional calculations
  • Metalloporphyrins
  • Oxidation
  • Polyoxometalates

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Computer-generated high-valent iron-oxo and manganese-oxo species with polyoxometalate ligands : How do they compare with the iron-oxo active species of heme enzymes? / De Visser, Samüel P.; Kumar, Devesh; Neumann, Ronny; Shaik, Sason.

In: Angewandte Chemie - International Edition, Vol. 43, No. 42, 25.10.2004, p. 5661-5665.

Research output: Contribution to journalArticle

@article{6b88e4db377d489ea09a49a747acc85e,
title = "Computer-generated high-valent iron-oxo and manganese-oxo species with polyoxometalate ligands: How do they compare with the iron-oxo active species of heme enzymes?",
abstract = "The structure and reactivity of high-valent FeVO and Mn VIO oxidation catalysts containing a polyoxometalate [PW 11O39]7- lacunary ligand (2) have been investigated by a computational study. Calculations have demonstrated there is an intriguing analogy between these species and the active species (1) of the enzyme cytochrome P450 (see scheme).",
keywords = "Cytochrome P450, Density functional calculations, Metalloporphyrins, Oxidation, Polyoxometalates",
author = "{De Visser}, {Sam{\"u}el P.} and Devesh Kumar and Ronny Neumann and Sason Shaik",
year = "2004",
month = "10",
day = "25",
doi = "10.1002/anie.200453867",
language = "English",
volume = "43",
pages = "5661--5665",
journal = "Angewandte Chemie - International Edition",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",
number = "42",

}

TY - JOUR

T1 - Computer-generated high-valent iron-oxo and manganese-oxo species with polyoxometalate ligands

T2 - How do they compare with the iron-oxo active species of heme enzymes?

AU - De Visser, Samüel P.

AU - Kumar, Devesh

AU - Neumann, Ronny

AU - Shaik, Sason

PY - 2004/10/25

Y1 - 2004/10/25

N2 - The structure and reactivity of high-valent FeVO and Mn VIO oxidation catalysts containing a polyoxometalate [PW 11O39]7- lacunary ligand (2) have been investigated by a computational study. Calculations have demonstrated there is an intriguing analogy between these species and the active species (1) of the enzyme cytochrome P450 (see scheme).

AB - The structure and reactivity of high-valent FeVO and Mn VIO oxidation catalysts containing a polyoxometalate [PW 11O39]7- lacunary ligand (2) have been investigated by a computational study. Calculations have demonstrated there is an intriguing analogy between these species and the active species (1) of the enzyme cytochrome P450 (see scheme).

KW - Cytochrome P450

KW - Density functional calculations

KW - Metalloporphyrins

KW - Oxidation

KW - Polyoxometalates

UR - http://www.scopus.com/inward/record.url?scp=8444244518&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=8444244518&partnerID=8YFLogxK

U2 - 10.1002/anie.200453867

DO - 10.1002/anie.200453867

M3 - Article

C2 - 15495193

AN - SCOPUS:8444244518

VL - 43

SP - 5661

EP - 5665

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

SN - 1433-7851

IS - 42

ER -