Ein Trispyrazolylborato-Eisen-Cysteinato-Komplex als funktionelles Modell für die Cystein-Dioxygenase

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im Januar 2012 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована в січні 2012

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Ein Trispyrazolylborato-Eisen- ...... ll für die Cystein-Dioxygenase

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Ein Trispyrazolylborato-Eisen- ...... ll für die Cystein-Dioxygenase

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Ein Trispyrazolylborato-Eisen- ...... ll für die Cystein-Dioxygenase

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Ein Trispyrazolylborato-Eisen- ...... ll für die Cystein-Dioxygenase

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Ein Trispyrazolylborato-Eisen- ...... ll für die Cystein-Dioxygenase

@en

Ein Trispyrazolylborato-Eisen- ...... ll für die Cystein-Dioxygenase

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P1476

Ein Trispyrazolylborato-Eisen- ...... ll für die Cystein-Dioxygenase

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P2093

Christian Limberg

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Christina Knispel

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Inke Siewert

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Lea Fohlmeister

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Madleen Sallmann

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P2860

Structure and mechanism of mouse cysteine dioxygenase

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

Sulfur versus iron oxidation in an iron-thiolate model complex

Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes

Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications.

High-valent iron(IV)-oxo complexes of heme and non-heme ligands in oxygenation reactions.

Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates.

Shape-selective interception by hydrocarbons of the O2-derived oxidant of a biomimetic nonheme iron complex.

Low-molecular-weight analogues of the soluble methane monooxygenase (sMMO): from the structural mimicking of resting states and intermediates to functional models.

O2 activation by bis(imino)pyridine iron(II)-thiolate complexes.

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2277-2280

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P31

scholarly article

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10.1002/ANGE.201107345

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P433

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P478

124

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P577

2012-01-27T00:00:00Z

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