MMO

P450 in wolf's clothing?

Research output: Contribution to journalReview article

60 Citations (Scopus)

Abstract

Methane monooxygenase (MMO) catalyzes the oxidation of stable hydrocarbons that are not attacked by cytochrome P450 monooxygenase. A key transient intermediate in the catalytic cycle of the soluble form of MMO termed compound Q (Q) has been trapped and characterized through spectroscopic comparisons with novel high valent model complexes. Q appears to contain a non-heme dinuclear Fe(IV) cluster bridged by at least two single oxygen atoms to form a so-called diamond core. Q has the ability to react directly with unactivated hydrocarbons to yield oxidized products. Several types of experiments indicate that this reaction involves formation of an intermediate, probably with radical character. This is consistent with a hydrogen atom abstraction mechanism analogous to that ascribed to cytochrome P450. However, these same experiments show that a pure hydrogen atom abstraction mechanism is unlikely for many substrates without an additional interaction between the intermediate that is formed and the high valent cluster. The results may be of general relevance to monooxygenase catalysis.

Original languageEnglish (US)
Pages (from-to)331-336
Number of pages6
JournalJournal of Biological Inorganic Chemistry
Volume3
Issue number3
DOIs
StatePublished - Jun 1 1998

Fingerprint

methane monooxygenase
Clothing
Hydrocarbons
Mixed Function Oxygenases
Cytochrome P-450 Enzyme System
Hydrogen
Trichosanthin
Atoms
Diamond
Catalysis
Oxygen
Experiments
Oxidation
Substrates

Keywords

  • Compound Q
  • Fe(IV)
  • Model complexes
  • Monooxygenase mechanism
  • Oxygen activation

Cite this

MMO : P450 in wolf's clothing? / Lipscomb, John D; Que, Larry.

In: Journal of Biological Inorganic Chemistry, Vol. 3, No. 3, 01.06.1998, p. 331-336.

Research output: Contribution to journalReview article

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title = "MMO: P450 in wolf's clothing?",
abstract = "Methane monooxygenase (MMO) catalyzes the oxidation of stable hydrocarbons that are not attacked by cytochrome P450 monooxygenase. A key transient intermediate in the catalytic cycle of the soluble form of MMO termed compound Q (Q) has been trapped and characterized through spectroscopic comparisons with novel high valent model complexes. Q appears to contain a non-heme dinuclear Fe(IV) cluster bridged by at least two single oxygen atoms to form a so-called diamond core. Q has the ability to react directly with unactivated hydrocarbons to yield oxidized products. Several types of experiments indicate that this reaction involves formation of an intermediate, probably with radical character. This is consistent with a hydrogen atom abstraction mechanism analogous to that ascribed to cytochrome P450. However, these same experiments show that a pure hydrogen atom abstraction mechanism is unlikely for many substrates without an additional interaction between the intermediate that is formed and the high valent cluster. The results may be of general relevance to monooxygenase catalysis.",
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AU - Que, Larry

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N2 - Methane monooxygenase (MMO) catalyzes the oxidation of stable hydrocarbons that are not attacked by cytochrome P450 monooxygenase. A key transient intermediate in the catalytic cycle of the soluble form of MMO termed compound Q (Q) has been trapped and characterized through spectroscopic comparisons with novel high valent model complexes. Q appears to contain a non-heme dinuclear Fe(IV) cluster bridged by at least two single oxygen atoms to form a so-called diamond core. Q has the ability to react directly with unactivated hydrocarbons to yield oxidized products. Several types of experiments indicate that this reaction involves formation of an intermediate, probably with radical character. This is consistent with a hydrogen atom abstraction mechanism analogous to that ascribed to cytochrome P450. However, these same experiments show that a pure hydrogen atom abstraction mechanism is unlikely for many substrates without an additional interaction between the intermediate that is formed and the high valent cluster. The results may be of general relevance to monooxygenase catalysis.

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