Pulsed EPR study of amino acid and tetrahydropterin binding in a tyrosine hydroxylase nitric oxide complex: evidence for substrate rearrangements in the formation of the oxygen-reactive complex.
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Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active siteSpectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study.Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.Characterization of unstable products of flavin- and pterin-dependent enzymes by continuous-flow mass spectrometry.
P2860
Pulsed EPR study of amino acid and tetrahydropterin binding in a tyrosine hydroxylase nitric oxide complex: evidence for substrate rearrangements in the formation of the oxygen-reactive complex.
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2013 nî lūn-bûn
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name
Pulsed EPR study of amino acid ...... f the oxygen-reactive complex.
@en
Pulsed EPR study of amino acid ...... f the oxygen-reactive complex.
@nl
type
label
Pulsed EPR study of amino acid ...... f the oxygen-reactive complex.
@en
Pulsed EPR study of amino acid ...... f the oxygen-reactive complex.
@nl
prefLabel
Pulsed EPR study of amino acid ...... f the oxygen-reactive complex.
@en
Pulsed EPR study of amino acid ...... f the oxygen-reactive complex.
@nl
P2093
P2860
P356
P1433
P1476
Pulsed EPR study of amino acid ...... of the oxygen-reactive complex
@en
P2093
Holly R Ellis
John McCracken
Matthew D Krzyaniak
Paul F Fitzpatrick
P2860
P304
P356
10.1021/BI4010914
P407
P50
P577
2013-11-14T00:00:00Z