Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases.
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Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylaseFormation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases.Mechanisms of tryptophan and tyrosine hydroxylase.Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.
P2860
Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases.
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2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
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2010年论文
@zh-cn
name
Single turnover kinetics of tr ...... matic amino acid hydroxylases.
@en
type
label
Single turnover kinetics of tr ...... matic amino acid hydroxylases.
@en
prefLabel
Single turnover kinetics of tr ...... matic amino acid hydroxylases.
@en
P2093
P2860
P356
P1433
P1476
Single turnover kinetics of tr ...... matic amino acid hydroxylases.
@en
P2093
Bekir Eser
Jorge Alex Pavon
Michaela T Huynh
Paul F Fitzpatrick
P2860
P304
P356
10.1021/BI100744R
P407
P577
2010-09-01T00:00:00Z