Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants

Subhasree Kal, Larry Que

Research output: Contribution to journalReview article

56 Citations (Scopus)

Abstract

The 2-His-1-carboxylate facial triad is a widely used scaffold to bind the iron center in mononuclear nonheme iron enzymes for activating dioxygen in a variety of oxidative transformations of metabolic significance. Since the 1990s, over a hundred different iron enzymes have been identified to use this platform. This structural motif consists of two histidines and the side chain carboxylate of an aspartate or a glutamate arranged in a facial array that binds iron(II) at the active site. This triad occupies one face of an iron-centered octahedron and makes the opposite face available for the coordination of O2 and, in many cases, substrate, allowing the tailoring of the iron-dioxygen chemistry to carry out a plethora of diverse reactions. Activated dioxygen-derived species involved in the enzyme mechanisms include iron(III)-superoxo, iron(III)-peroxo, and high-valent iron(IV)-oxo intermediates. In this article, we highlight the major crystallographic, spectroscopic, and mechanistic advances of the past 20 years that have significantly enhanced our understanding of the mechanisms of O2 activation and the key roles played by iron-based oxidants.

Original languageEnglish (US)
Pages (from-to)339-365
Number of pages27
JournalJournal of Biological Inorganic Chemistry
Volume22
Issue number2-3
DOIs
StatePublished - Apr 1 2017

Fingerprint

Oxidants
Iron
Chemical activation
Oxygen
Enzymes
Histidine
Aspartic Acid
Scaffolds
Glutamic Acid
Catalytic Domain
Substrates

Keywords

  • 2-His-1-carboxylate facial triad
  • Halogenases
  • Nonheme iron enzymes
  • O activation
  • Pterin-dependent hydroxylases
  • Rieske oxygenases
  • α-Ketoglutarate-dependent enzymes

Cite this

Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants. / Kal, Subhasree; Que, Larry.

In: Journal of Biological Inorganic Chemistry, Vol. 22, No. 2-3, 01.04.2017, p. 339-365.

Research output: Contribution to journalReview article

@article{f4929de150ea4828943705d8c6585a52,
title = "Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants",
abstract = "The 2-His-1-carboxylate facial triad is a widely used scaffold to bind the iron center in mononuclear nonheme iron enzymes for activating dioxygen in a variety of oxidative transformations of metabolic significance. Since the 1990s, over a hundred different iron enzymes have been identified to use this platform. This structural motif consists of two histidines and the side chain carboxylate of an aspartate or a glutamate arranged in a facial array that binds iron(II) at the active site. This triad occupies one face of an iron-centered octahedron and makes the opposite face available for the coordination of O2 and, in many cases, substrate, allowing the tailoring of the iron-dioxygen chemistry to carry out a plethora of diverse reactions. Activated dioxygen-derived species involved in the enzyme mechanisms include iron(III)-superoxo, iron(III)-peroxo, and high-valent iron(IV)-oxo intermediates. In this article, we highlight the major crystallographic, spectroscopic, and mechanistic advances of the past 20 years that have significantly enhanced our understanding of the mechanisms of O2 activation and the key roles played by iron-based oxidants.",
keywords = "2-His-1-carboxylate facial triad, Halogenases, Nonheme iron enzymes, O activation, Pterin-dependent hydroxylases, Rieske oxygenases, α-Ketoglutarate-dependent enzymes",
author = "Subhasree Kal and Larry Que",
year = "2017",
month = "4",
day = "1",
doi = "10.1007/s00775-016-1431-2",
language = "English (US)",
volume = "22",
pages = "339--365",
journal = "Journal of Biological Inorganic Chemistry",
issn = "0949-8257",
publisher = "Springer Verlag",
number = "2-3",

}

TY - JOUR

T1 - Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants

AU - Kal, Subhasree

AU - Que, Larry

PY - 2017/4/1

Y1 - 2017/4/1

N2 - The 2-His-1-carboxylate facial triad is a widely used scaffold to bind the iron center in mononuclear nonheme iron enzymes for activating dioxygen in a variety of oxidative transformations of metabolic significance. Since the 1990s, over a hundred different iron enzymes have been identified to use this platform. This structural motif consists of two histidines and the side chain carboxylate of an aspartate or a glutamate arranged in a facial array that binds iron(II) at the active site. This triad occupies one face of an iron-centered octahedron and makes the opposite face available for the coordination of O2 and, in many cases, substrate, allowing the tailoring of the iron-dioxygen chemistry to carry out a plethora of diverse reactions. Activated dioxygen-derived species involved in the enzyme mechanisms include iron(III)-superoxo, iron(III)-peroxo, and high-valent iron(IV)-oxo intermediates. In this article, we highlight the major crystallographic, spectroscopic, and mechanistic advances of the past 20 years that have significantly enhanced our understanding of the mechanisms of O2 activation and the key roles played by iron-based oxidants.

AB - The 2-His-1-carboxylate facial triad is a widely used scaffold to bind the iron center in mononuclear nonheme iron enzymes for activating dioxygen in a variety of oxidative transformations of metabolic significance. Since the 1990s, over a hundred different iron enzymes have been identified to use this platform. This structural motif consists of two histidines and the side chain carboxylate of an aspartate or a glutamate arranged in a facial array that binds iron(II) at the active site. This triad occupies one face of an iron-centered octahedron and makes the opposite face available for the coordination of O2 and, in many cases, substrate, allowing the tailoring of the iron-dioxygen chemistry to carry out a plethora of diverse reactions. Activated dioxygen-derived species involved in the enzyme mechanisms include iron(III)-superoxo, iron(III)-peroxo, and high-valent iron(IV)-oxo intermediates. In this article, we highlight the major crystallographic, spectroscopic, and mechanistic advances of the past 20 years that have significantly enhanced our understanding of the mechanisms of O2 activation and the key roles played by iron-based oxidants.

KW - 2-His-1-carboxylate facial triad

KW - Halogenases

KW - Nonheme iron enzymes

KW - O activation

KW - Pterin-dependent hydroxylases

KW - Rieske oxygenases

KW - α-Ketoglutarate-dependent enzymes

UR - http://www.scopus.com/inward/record.url?scp=85009216265&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85009216265&partnerID=8YFLogxK

U2 - 10.1007/s00775-016-1431-2

DO - 10.1007/s00775-016-1431-2

M3 - Review article

C2 - 28074299

AN - SCOPUS:85009216265

VL - 22

SP - 339

EP - 365

JO - Journal of Biological Inorganic Chemistry

JF - Journal of Biological Inorganic Chemistry

SN - 0949-8257

IS - 2-3

ER -