Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase

被引:143
作者
Eser, Bekir E.
Barr, Eric W.
Frantorn, Patrick A.
Saleh, Lana
Bollinger, J. Martin, Jr. [1 ]
Krebs, Carsten
Fitzpatrick, Paul F.
机构
[1] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA
[2] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
[3] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
[4] Penn State Univ, Dept Chem, University Pk, PA 16802 USA
关键词
D O I
10.1021/ja074446s
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Tyrosine hydroxylase, a member of the aromatic amino acid hydroxylase family, uses a mononuclear Fe(H) and tetrahydropterin for hydroxylation of tyrosine to dihydroxyphenylalanine. Rapid-freeze quench Mossbauer spectroscopy has now provided direct evidence for the presence of an Fe(IV) intermediate in the reaction catalyzed by tyrosine hydroxylase. Rapid-quench techniques provide support for the kinetic competence of this species as the hydroxylating intermediate. This is the first direct evidence for a mononuclear Fe(IV) intermediate in an enzymatic aromatic hydroxylation reaction.
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收藏
页码:11334 / +
页数:3
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