Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex

Jan Uwe Rohde, Jun Hee In, Mi Hee Lim, William W. Brennessel, Michael R. Bukowski, Audria Stubna, Eckard Münck, Wonwoo Nam, Larry Que

Research output: Contribution to journalArticle

664 Citations (Scopus)

Abstract

Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.

Original languageEnglish (US)
Pages (from-to)1037-1039
Number of pages3
JournalScience
Volume299
Issue number5609
DOIs
StatePublished - Feb 14 2003

Fingerprint

Iron
Oxygen
Ligands
Catalysis
Heme
Enzymes
ferryl iron

Cite this

Rohde, J. U., In, J. H., Lim, M. H., Brennessel, W. W., Bukowski, M. R., Stubna, A., ... Que, L. (2003). Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex. Science, 299(5609), 1037-1039. https://doi.org/10.1126/science.299.5609.1037

Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex. / Rohde, Jan Uwe; In, Jun Hee; Lim, Mi Hee; Brennessel, William W.; Bukowski, Michael R.; Stubna, Audria; Münck, Eckard; Nam, Wonwoo; Que, Larry.

In: Science, Vol. 299, No. 5609, 14.02.2003, p. 1037-1039.

Research output: Contribution to journalArticle

Rohde, JU, In, JH, Lim, MH, Brennessel, WW, Bukowski, MR, Stubna, A, Münck, E, Nam, W & Que, L 2003, 'Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex', Science, vol. 299, no. 5609, pp. 1037-1039. https://doi.org/10.1126/science.299.5609.1037
Rohde JU, In JH, Lim MH, Brennessel WW, Bukowski MR, Stubna A et al. Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex. Science. 2003 Feb 14;299(5609):1037-1039. https://doi.org/10.1126/science.299.5609.1037
Rohde, Jan Uwe ; In, Jun Hee ; Lim, Mi Hee ; Brennessel, William W. ; Bukowski, Michael R. ; Stubna, Audria ; Münck, Eckard ; Nam, Wonwoo ; Que, Larry. / Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex. In: Science. 2003 ; Vol. 299, No. 5609. pp. 1037-1039.
@article{8531bb8ae2a04744b3267eb0686d9ab9,
title = "Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex",
abstract = "Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.",
author = "Rohde, {Jan Uwe} and In, {Jun Hee} and Lim, {Mi Hee} and Brennessel, {William W.} and Bukowski, {Michael R.} and Audria Stubna and Eckard M{\"u}nck and Wonwoo Nam and Larry Que",
year = "2003",
month = "2",
day = "14",
doi = "10.1126/science.299.5609.1037",
language = "English (US)",
volume = "299",
pages = "1037--1039",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5609",

}

TY - JOUR

T1 - Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex

AU - Rohde, Jan Uwe

AU - In, Jun Hee

AU - Lim, Mi Hee

AU - Brennessel, William W.

AU - Bukowski, Michael R.

AU - Stubna, Audria

AU - Münck, Eckard

AU - Nam, Wonwoo

AU - Que, Larry

PY - 2003/2/14

Y1 - 2003/2/14

N2 - Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.

AB - Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.

UR - http://www.scopus.com/inward/record.url?scp=0037436143&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037436143&partnerID=8YFLogxK

U2 - 10.1126/science.299.5609.1037

DO - 10.1126/science.299.5609.1037

M3 - Article

C2 - 12586936

AN - SCOPUS:0037436143

VL - 299

SP - 1037

EP - 1039

JO - Science

JF - Science

SN - 0036-8075

IS - 5609

ER -