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- W2000968981 endingPage "518" @default.
- W2000968981 startingPage "507" @default.
- W2000968981 abstract "The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented." @default.
- W2000968981 created "2016-06-24" @default.
- W2000968981 creator A5050548366 @default.
- W2000968981 creator A5053309916 @default.
- W2000968981 creator A5066630519 @default.
- W2000968981 creator A5081446055 @default.
- W2000968981 date "2006-04-01" @default.
- W2000968981 modified "2023-09-27" @default.
- W2000968981 title "The status of high-valent metal oxo complexes in the P450 cytochromes" @default.
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