G
Gunhild Layer
Researcher at University of Freiburg
Publications - 48
Citations - 2273
Gunhild Layer is an academic researcher from University of Freiburg. The author has contributed to research in topics: Heme & Cofactor. The author has an hindex of 21, co-authored 43 publications receiving 1980 citations. Previous affiliations of Gunhild Layer include Braunschweig University of Technology & Leipzig University.
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Journal ArticleDOI
Iron-Sulfur Cluster Biosynthesis CHARACTERIZATION OF ESCHERICHIA COLI CYaY AS AN IRON DONOR FOR THE ASSEMBLY OF [2Fe-2S] CLUSTERS IN THE SCAFFOLD IscU
TL;DR: A specific interaction between CyaY and IscS, a cysteine desulfurase participating in iron-sulfur cluster assembly is demonstrated for the first time, pointing toward a link between CyY and [Fe-S] cluster biosynthesis.
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Structure and function of enzymes in heme biosynthesis.
TL;DR: This review summarizes the current understanding of the structure–function relationship for all heme biosynthetic enzymes and their potential interactions in the cell.
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Crystal Structure of Coproporphyrinogen III Oxidase Reveals Cofactor Geometry of Radical Sam Enzymes
TL;DR: The structure of HemN reveals the cofactor geometry required for Radical SAM catalysis and sets the stage for the development of inhibitors with antibacterial function due to the uniquely bacterial occurrence of the enzyme.
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SufE Transfers Sulfur from SufS to SufB for Iron-Sulfur Cluster Assembly
Gunhild Layer,S. Aparna Gaddam,Carla Ayala-Castro,Sandrine Ollagnier de Choudens,David Lascoux,Marc Fontecave,F. Wayne Outten +6 more
TL;DR: It is found that SufE in turn interacts with the SufB protein for sulfur transfer to that protein if SufC is present, which provides the first evidence of a novel site for Fe-S cluster assembly in theSufBCD complex.
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Oxygen-independent Coproporphyrinogen-III Oxidase HemN from Escherichia coli
TL;DR: Sofia et al. as discussed by the authors used an anaerobic enzyme assay to demonstrate for the first time in vitro coproporphyrinogen-III oxidase activity for recombinant purified HemN.