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Gunhild Layer (1975-)

Biochemikerin

Name	Gunhild Layer
Time	1975- (Date of birth and death)
Place	Deutschland
Academic degree	Prof. Dr. (Naturwiss. Fakultät der Techn. Univ. Braunschweig) (2004)
Profession	Biochemikerin (characteristic profession)
Variant	Gunhild Monika Layer
Further information	seit 6/2018: Professorin für Pharmazeutische Biologie am Institut für Pharmazeutische Wissenschaften der Fakultät für Chemie und Pharmazie der Albert-Ludwigs-Universität Freiburg Habil. Lehrgebiete Biochemie und Mikrobiologie an der Techn. Univ. Braunschweig
Record type	Person
GND-Identifier	129524468
Record ID	129524468
Involved in show all The small membrane protein CcoS is involved in cofactor insertion into the cbb3-type cytochrome c oxidase Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis Trapping the substrate radical of heme synthase AhbD Untersuchungen von Bienen auf Streptomyceten und deren produzierten Naturstoffe Biomimetic S ‐Adenosylmethionine Regeneration Starting from Multiple Byproducts Enables Biocatalytic Alkylation with Radical SAM Enzymes ** anaerobic cyclase BchE from Rhodobacter capsulatus is a cobalamin-dependent radical SAM enzyme Biomimetic S-adenosylmethionine regeneration starting from multiple byproducts enables biocatalytic alkylation with radical sam enzymes The Radical SAM heme synthase AhbD from Methanosarcina barkeri contains two auxiliary [4Fe-4S] clusters A cobalamin‐dependent radical SAM enzyme catalyzes the unique Cα‐methylation of glutamine in methyl‐coenzyme M reductase Charakterisierung der Eisen-Schwefel-Cluster der Häm-Synthase AhbD aus Methanosarcina barkeri Design und Entwicklung eines rekombinanten, modularen Hydrogelsystems auf Basis humaner Proteinpolymere für biomedizinische Anwendungen Radical SAM enzymes involved in tetrapyrrole biosynthesis and insertion Biochemische Untersuchungen zu NirN und NirF aus Pseudomonas aeruginosa Crystal structure of NirF: insights into its role in heme d1 biosynthesis Investigation and analysis on the biosynthesis of curacozole and foxicin Nitrogenase-like Biosynthesis of (Bacterio)chlorophylls Structural biology of Pseudomonas aeruginosa enzymes involved in heme d1 biosynthesis Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase Front Cover: Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase (ChemBioChem 12/2020) Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase Identification and characterization of a bacterial core methionine synthase Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase Der letzte Biosyntheseschritt des Nitritreduktasekofaktors Häm d1 in Pseudomonas aeruginosa Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase Strukturelle und funktionelle Charakterisierung der Sirohäm-Decarboxylasen NirDLGH aus Pseudomonas aeruginosa und NirDL aus Hydrogenobacter thermophilus The auxiliary [4Fe–4S] cluster of the Radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer NirN protein from pseudomonas aeruginosa is a novel electron-bifurcating dehydrogenase catalyzing the last step of heme d1 biosynthesis The alternative route to heme in the methanogenic archaeon methanosarcina barkeri Maturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF Biosynthesis of iron-sulfur clusters and tetrapyrroles in microorganisms Crystal Structure of the heme d1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-Adenosyl-l-methionine-dependent Uroporphyrinogen III methyltransferases A Novel Pathway for the Biosynthesis of Heme inArchaea: Genome-Based Bioinformatic Predictions and Experimental Evidence Iron-sulfur (Fe-S) cluster assembly SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly Iron-sulfur cluster biosynthesis : : characterization of Escherichia coli cyay as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN : : functional features of the [4Fe-4S] cluser and the two bound S-adenosyl-L-methionines Structure and function of the oxygen independent coproporphyrinogen III oxidase HemN from Escherichia coli Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese

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Gunhild Layer (1975-)

The small membrane protein CcoS is involved in cofactor insertion into the cbb3-type cytochrome c oxidase

Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis

Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis

Trapping the substrate radical of heme synthase AhbD

Untersuchungen von Bienen auf Streptomyceten und deren produzierten Naturstoffe

Biomimetic S ‐Adenosylmethionine Regeneration Starting from Multiple Byproducts Enables Biocatalytic Alkylation with Radical SAM Enzymes **

anaerobic cyclase BchE from Rhodobacter capsulatus is a cobalamin-dependent radical SAM enzyme

Biomimetic S-adenosylmethionine regeneration starting from multiple byproducts enables biocatalytic alkylation with radical sam enzymes

The Radical SAM heme synthase AhbD from Methanosarcina barkeri contains two auxiliary [4Fe-4S] clusters

A cobalamin‐dependent radical SAM enzyme catalyzes the unique Cα‐methylation of glutamine in methyl‐coenzyme M reductase

Charakterisierung der Eisen-Schwefel-Cluster der Häm-Synthase AhbD aus Methanosarcina barkeri

Design und Entwicklung eines rekombinanten, modularen Hydrogelsystems auf Basis humaner Proteinpolymere für biomedizinische Anwendungen

Radical SAM enzymes involved in tetrapyrrole biosynthesis and insertion

Biochemische Untersuchungen zu NirN und NirF aus Pseudomonas aeruginosa

Crystal structure of NirF: insights into its role in heme d1 biosynthesis

Investigation and analysis on the biosynthesis of curacozole and foxicin

Nitrogenase-like Biosynthesis of (Bacterio)chlorophylls

Structural biology of Pseudomonas aeruginosa enzymes involved in heme d1 biosynthesis

Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase

Front Cover: Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase (ChemBioChem 12/2020)

Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase

Identification and characterization of a bacterial core methionine synthase

Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase

Der letzte Biosyntheseschritt des Nitritreduktasekofaktors Häm d1 in Pseudomonas aeruginosa

Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase

Strukturelle und funktionelle Charakterisierung der Sirohäm-Decarboxylasen NirDLGH aus Pseudomonas aeruginosa und NirDL aus Hydrogenobacter thermophilus

The auxiliary [4Fe–4S] cluster of the Radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer

NirN protein from pseudomonas aeruginosa is a novel electron-bifurcating dehydrogenase catalyzing the last step of heme d1 biosynthesis

The alternative route to heme in the methanogenic archaeon methanosarcina barkeri

Maturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF

Biosynthesis of iron-sulfur clusters and tetrapyrroles in microorganisms

Crystal Structure of the heme d1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-Adenosyl-l-methionine-dependent Uroporphyrinogen III methyltransferases

A Novel Pathway for the Biosynthesis of Heme inArchaea: Genome-Based Bioinformatic Predictions and Experimental Evidence

Iron-sulfur (Fe-S) cluster assembly

SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly

Iron-sulfur cluster biosynthesis : : characterization of Escherichia coli cyay as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU

The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN

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

Structure and function of the oxygen independent coproporphyrinogen III oxidase HemN from Escherichia coli

Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese