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Person

Lena J. Daumann (1983-)

Chemikerin

Name	Lena J. Daumann
Zeit	1983- (Lebensdaten)
Ort	Emmendingen (Geburtsort) München (Wirkungsort) Düsseldorf (Wirkungsort) Deutschland
Geschlecht	weiblich
Akademischer Grad bzw. Titel	Prof. Dr.
Beruf	Chemikerin (charakteristischer Beruf) Hochschullehrerin
Variante	Lena Daumann Lena Josefine Daumann (vollständiger Name)
Beziehung	Heinrich-Heine-Universität Düsseldorf. Lehrstuhl für Bioanorganische Chemie Ludwig-Maximilians-Universität München
Themengebiet	Personen zu Bibliothek, Information und Dokumentation Personen zu Chemie
Weitere Angaben	Jan 2010 - Aug 2013 University of Queensland, School of Chemistry and Molecular Biosciences Brisbane, Australia, PhD student.
Quelle	https://www.math-nat-fak.hhu.de/aktuelles-1/aktuelles-detailansicht/dr-lena-daumann-neue-w3-professorin-fuer-bioanorganische-chemie (Stand: 16.07.2024)
Datensatztyp	Person
GND-Nummer	1164536869
Datensatz-ID	1164536869
Beteiligt an alle anzeigen Assessing Lanthanide‐Dependent Methanol Dehydrogenase Activity: The Assay Matters Assessing Lanthanide‐Dependent Methanol Dehydrogenase Activity: The Assay Matters Minor Actinides Can Replace Essential Lanthanides in Bacterial Life Minor Actinides Can Replace Essential Lanthanides in Bacterial Life Minor Actinides Can Replace Essential Lanthanides in Bacterial Life Minor Actinides Can Replace Essential Lanthanides in Bacterial Life Modular Synthesis of New Pyrroloquinoline Quinone Derivatives Spectroscopic and in vitro Investigations of Fe 2+/α‐Ketoglutarate‐Dependent Enzymes Involved in Nucleic Acid Repair and Modification TET‐Like Oxidation in 5‐Methylcytosine and Derivatives: A Computational and Experimental Study TET‐Like Oxidation in 5‐Methylcytosine and Derivatives: A Computational and Experimental Study Biomimetic Iron Complex Achieves TET Enzyme Reactivity Biomimetic Iron Complex Achieves TET Enzyme Reactivity Pyrroloquinoline Quinone Aza‐Crown Ether Complexes as Biomimetics for Lanthanide and Calcium Dependent Alcohol Dehydrogenases ** Formation of Cisplatin Adducts with the Epigenetically Relevant Nucleobase 5‐Methylcytosine Cover Feature: Formation of Cisplatin Adducts with the Epigenetically Relevant Nucleobase 5‐Methylcytosine (Eur. J. Inorg. Chem. 1/2021) Understanding the chemistry of the artificial electron acceptors PES, PMS, DCPIP and Wurster’s Blue in methanol dehydrogenase assays The Earlier the Better: Structural Analysis and Separation of Lanthanides with Pyrroloquinoline Quinone Cover Feature: The Earlier the Better: Structural Analysis and Separation of Lanthanides with Pyrroloquinoline Quinone (Chem. Eur. J. 44/2020) Crystal structure of a calcium(II)–pyrroloquinoline quinone (PQQ) complex outside a protein environment Crystal structure of a calcium(II)–pyrroloquinoline quinone (PQQ) complex outside a protein environment1 Sulfur mustard alkylates steroid hormones and impacts hormone function in vitro Corrigendum: 5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex 5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex † Cover Feature: 5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex (Chem. Eur. J. 52/2019) Electrocatalysis of a Europium‐Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron‐Acceptor Cytochrome c GJ Cover Feature: Electrocatalysis of a Europium‐Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron‐Acceptor Cytochrome c GJ (Chem. Eur. J. 37/2019) Essenziell und weitverbreitet: Lanthanoid‐Metalloproteine Essential and Ubiquitous: The Emergence of Lanthanide Metallobiochemistry Die vier Neuen: Nihonium, Moscovium, Tenness und Oganesson Correlation of Structural and Magnetic Properties in a Set of Mononuclear Lanthanide Complexes Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site Front Cover: Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site (ChemBioChem 11/2018) Impact of the lanthanide contraction on the activity of a lanthanide-dependent methanol dehydrogenase - a kinetic and DFT study Dinuclear Cobalt (II) Complexes as Metallo‐β‐lactamase Mimics

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Katalog der Deutschen Nationalbibliothek

Assessing Lanthanide‐Dependent Methanol Dehydrogenase Activity: The Assay Matters

Assessing Lanthanide‐Dependent Methanol Dehydrogenase Activity: The Assay Matters

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life **

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life **

Modular Synthesis of New Pyrroloquinoline Quinone Derivatives

Spectroscopic and in vitro Investigations of Fe 2+/α‐Ketoglutarate‐Dependent Enzymes Involved in Nucleic Acid Repair and Modification

TET‐Like Oxidation in 5‐Methylcytosine and Derivatives: A Computational and Experimental Study

TET‐Like Oxidation in 5‐Methylcytosine and Derivatives: A Computational and Experimental Study

Biomimetic Iron Complex Achieves TET Enzyme Reactivity **

Biomimetic Iron Complex Achieves TET Enzyme Reactivity **

Pyrroloquinoline Quinone Aza‐Crown Ether Complexes as Biomimetics for Lanthanide and Calcium Dependent Alcohol Dehydrogenases **

Formation of Cisplatin Adducts with the Epigenetically Relevant Nucleobase 5‐Methylcytosine

Cover Feature: Formation of Cisplatin Adducts with the Epigenetically Relevant Nucleobase 5‐Methylcytosine (Eur. J. Inorg. Chem. 1/2021)

Understanding the chemistry of the artificial electron acceptors PES, PMS, DCPIP and Wurster’s Blue in methanol dehydrogenase assays

The Earlier the Better: Structural Analysis and Separation of Lanthanides with Pyrroloquinoline Quinone

Cover Feature: The Earlier the Better: Structural Analysis and Separation of Lanthanides with Pyrroloquinoline Quinone (Chem. Eur. J. 44/2020)

Crystal structure of a calcium(II)–pyrroloquinoline quinone (PQQ) complex outside a protein environment

Crystal structure of a calcium(II)–pyrroloquinoline quinone (PQQ) complex outside a protein environment1

Sulfur mustard alkylates steroid hormones and impacts hormone function in vitro

Corrigendum: 5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex

5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex †

Cover Feature: 5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex (Chem. Eur. J. 52/2019)

Electrocatalysis of a Europium‐Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron‐Acceptor Cytochrome c GJ

Cover Feature: Electrocatalysis of a Europium‐Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron‐Acceptor Cytochrome c GJ (Chem. Eur. J. 37/2019)

Essenziell und weitverbreitet: Lanthanoid‐Metalloproteine

Essential and Ubiquitous: The Emergence of Lanthanide Metallobiochemistry

Die vier Neuen: Nihonium, Moscovium, Tenness und Oganesson

Correlation of Structural and Magnetic Properties in a Set of Mononuclear Lanthanide Complexes

Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site

Front Cover: Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site (ChemBioChem 11/2018)

Impact of the lanthanide contraction on the activity of a lanthanide-dependent methanol dehydrogenase - a kinetic and DFT study

Dinuclear Cobalt (II) Complexes as Metallo‐β‐lactamase Mimics

Katalog der Deutschen Nationalbibliothek

Lena J. Daumann (1983-)

Assessing Lanthanide‐Dependent Methanol Dehydrogenase Activity: The Assay Matters

Assessing Lanthanide‐Dependent Methanol Dehydrogenase Activity: The Assay Matters

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life **

Minor Actinides Can Replace Essential Lanthanides in Bacterial Life **

Modular Synthesis of New Pyrroloquinoline Quinone Derivatives

Spectroscopic and in vitro Investigations of Fe 2+/α‐Ketoglutarate‐Dependent Enzymes Involved in Nucleic Acid Repair and Modification

TET‐Like Oxidation in 5‐Methylcytosine and Derivatives: A Computational and Experimental Study

TET‐Like Oxidation in 5‐Methylcytosine and Derivatives: A Computational and Experimental Study

Biomimetic Iron Complex Achieves TET Enzyme Reactivity **

Biomimetic Iron Complex Achieves TET Enzyme Reactivity **

Pyrroloquinoline Quinone Aza‐Crown Ether Complexes as Biomimetics for Lanthanide and Calcium Dependent Alcohol Dehydrogenases **

Formation of Cisplatin Adducts with the Epigenetically Relevant Nucleobase 5‐Methylcytosine

Cover Feature: Formation of Cisplatin Adducts with the Epigenetically Relevant Nucleobase 5‐Methylcytosine (Eur. J. Inorg. Chem. 1/2021)

Understanding the chemistry of the artificial electron acceptors PES, PMS, DCPIP and Wurster’s Blue in methanol dehydrogenase assays

The Earlier the Better: Structural Analysis and Separation of Lanthanides with Pyrroloquinoline Quinone

Cover Feature: The Earlier the Better: Structural Analysis and Separation of Lanthanides with Pyrroloquinoline Quinone (Chem. Eur. J. 44/2020)

Crystal structure of a calcium(II)–pyrroloquinoline quinone (PQQ) complex outside a protein environment

Crystal structure of a calcium(II)–pyrrolo­quinoline quinone (PQQ) complex outside a protein environment1

Sulfur mustard alkylates steroid hormones and impacts hormone function in vitro

Corrigendum: 5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex

5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex †

Cover Feature: 5‐Methylcytosine is Oxidized to the Natural Metabolites of TET Enzymes by a Biomimetic Iron (IV)‐Oxo Complex (Chem. Eur. J. 52/2019)

Electrocatalysis of a Europium‐Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron‐Acceptor Cytochrome c GJ

Cover Feature: Electrocatalysis of a Europium‐Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron‐Acceptor Cytochrome c GJ (Chem. Eur. J. 37/2019)

Essenziell und weitverbreitet: Lanthanoid‐Metalloproteine

Essential and Ubiquitous: The Emergence of Lanthanide Metallobiochemistry

Die vier Neuen: Nihonium, Moscovium, Tenness und Oganesson

Correlation of Structural and Magnetic Properties in a Set of Mononuclear Lanthanide Complexes

Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site

Front Cover: Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site (ChemBioChem 11/2018)

Impact of the lanthanide contraction on the activity of a lanthanide-dependent methanol dehydrogenase - a kinetic and DFT study

Dinuclear Cobalt (II) Complexes as Metallo‐β‐lactamase Mimics

Crystal structure of a calcium(II)–pyrroloquinoline quinone (PQQ) complex outside a protein environment1