The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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Go it alone: four-electron oxidations by mononuclear non-heme iron enzymes.

P2860

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P2860

The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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2011 nî lūn-bûn

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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P1476

The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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P2093

Chengbu Liu

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Dongju Zhang

http://www.w3.org/2001/XMLSchema#string

Jun Gao

http://www.w3.org/2001/XMLSchema#string

Yongjun Liu

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Water induces a structural conversion and accelerates the oxygenation of carboxylate-bridged non-heme diiron enzyme synthetic analogues.

The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes.

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1014-1024

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scholarly article

P356

10.1039/C1OB06221B

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Likai Du

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2011-12-06T00:00:00Z

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51854414

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22143311

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The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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P2860

P2860

The reaction mechanism of hydroxyethylphosphonate dioxygenase: a QM/MM study.

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type

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P1433

P1476

P2093

P2860

P304

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P356

P433

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P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698