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Volker Schünemann

Physiker

Name	Volker Schünemann
Ort	Technische Universität Kaiserslautern, Lehrstuhl Biophysik/Experimentalphysik (Wirkungsort)
Akademischer Grad bzw. Titel	Prof., Dr.
Beruf	Physiker (charakteristischer Beruf)
Variante	... Schünemann
Datensatztyp	Person
GND-Nummer	132183668
Datensatz-ID	132183668
Beteiligt an alle anzeigen Publisher Correction: TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster Advanced Characterization of Fe-N-C Catalysts using Nuclear Resonance Techniques Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1 Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors Interpretation of Nuclear Resonant Vibrational Spectra of Rubredoxin Using a Combined Quantum Mechanics and Molecular Mechanics Approach Mössbauer spectroscopic studies of the six‐coordinate heme—nitric oxide complex of iron (III) octaethylporphyrin N ‐methylimidazole, the first model of the nitrophorin—no complexes Low‐Temperature EPR and Mössbauer Spectroscopy of Two Cytochromes with His–Met Axial Coordination Exhibiting HALS Signals † Topologic Equivalents of Coronands, Cryptands and Their Inclusion Complexes: Synthesis, Structure and Properties of {2}‐Metallacryptands and {2}‐Metallacryptates † ‡ Molecular Structure of the Chloroiron (III) Derivative of the meso ‐Unsubstituted 2,7,12,17‐Tetramethyl‐3,8,13,18‐tetramesitylporphyrin and Weak Ferromagnetic Exchange Interactions in the A 1u Oxoiron (IV) Porphyrin π Radical Cation Complex Ein neutraler, tripelhelicaler, gemischtvalenter μ 3 ‐Oxotrieisen‐Komplex † Achtfach koordinierte Eisen (II)‐ und Eisen (III)‐Ionen in Komplexen mit verzerrt dodekaedrischen FeN 8 ‐Koordinationsgeometrien: Synthesen und Strukturen von Bis (2,11‐diaza‐(3.3)(2,6) pyridinophan) eisen‐Komplexen † Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe–4S] protein Trinuclear Oxo‐Centered Iron and Iron/Nickel Clusters – Ligand‐Controlled Homo/Hetero Valency Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450 Biophysik : eine Einführung ; mit 13 Tabellen Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN : : functional features of the [4Fe-4S] cluser and the two bound S-adenosyl-L-methionines A Neutral, Triple‐Helical, Trinuclear, Oxo‐Centered Mixed‐Valence Iron Complex † ‡ Sulfide Oxidation by Hydrogen Peroxide Catalyzed by Iron Complexes: Two Metal Centers Are Better Than One A Diferric Peroxo Complex with an Unprecedented Spin Configuration: An S =2 System Arising from an S =5/2, 1/2 Pair Iron coordination geometry in full-length, truncated, and dehydrated forms of human tyrosine hydroxylase studied by Mössbauer and X-ray absorption spectroscopy Magnetisches und katalytisches Verhalten von Eisenteilchen im Zeolith NaX

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Katalog der Deutschen Nationalbibliothek

Volker Schünemann

Publisher Correction: TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster

TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster

TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster

Advanced Characterization of Fe-N-C Catalysts using Nuclear Resonance Techniques

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors

Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors

Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors

Interpretation of Nuclear Resonant Vibrational Spectra of Rubredoxin Using a Combined Quantum Mechanics and Molecular Mechanics Approach

Mössbauer spectroscopic studies of the six‐coordinate heme—nitric oxide complex of iron (III) octaethylporphyrin N ‐methylimidazole, the first model of the nitrophorin—no complexes

Low‐Temperature EPR and Mössbauer Spectroscopy of Two Cytochromes with His–Met Axial Coordination Exhibiting HALS Signals †

Topologic Equivalents of Coronands, Cryptands and Their Inclusion Complexes: Synthesis, Structure and Properties of {2}‐Metallacryptands and {2}‐Metallacryptates † ‡

Molecular Structure of the Chloroiron (III) Derivative of the meso ‐Unsubstituted 2,7,12,17‐Tetramethyl‐3,8,13,18‐tetramesitylporphyrin and Weak Ferromagnetic Exchange Interactions in the A 1u Oxoiron (IV) Porphyrin π Radical Cation Complex

Ein neutraler, tripelhelicaler, gemischtvalenter μ 3 ‐Oxotrieisen‐Komplex †

Achtfach koordinierte Eisen (II)‐ und Eisen (III)‐Ionen in Komplexen mit verzerrt dodekaedrischen FeN 8 ‐Koordinationsgeometrien: Synthesen und Strukturen von Bis (2,11‐diaza‐(3.3)(2,6) pyridinophan) eisen‐Komplexen †

Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe–4S] protein

Trinuclear Oxo‐Centered Iron and Iron/Nickel Clusters – Ligand‐Controlled Homo/Hetero Valency

Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450

Biophysik : eine Einführung ; mit 13 Tabellen

Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN : : functional features of the [4Fe-4S] cluser and the two bound S-adenosyl-L-methionines

A Neutral, Triple‐Helical, Trinuclear, Oxo‐Centered Mixed‐Valence Iron Complex † ‡

Sulfide Oxidation by Hydrogen Peroxide Catalyzed by Iron Complexes: Two Metal Centers Are Better Than One

A Diferric Peroxo Complex with an Unprecedented Spin Configuration: An S =2 System Arising from an S =5/2, 1/2 Pair

Iron coordination geometry in full-length, truncated, and dehydrated forms of human tyrosine hydroxylase studied by Mössbauer and X-ray absorption spectroscopy

Magnetisches und katalytisches Verhalten von Eisenteilchen im Zeolith NaX