J
Julian Esselborn
Researcher at Ruhr University Bochum
Publications - 16
Citations - 1459
Julian Esselborn is an academic researcher from Ruhr University Bochum. The author has contributed to research in topics: Active site & Hydrogenase. The author has an hindex of 11, co-authored 15 publications receiving 1202 citations. Previous affiliations of Julian Esselborn include University of California, San Diego.
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Journal ArticleDOI
Biomimetic assembly and activation of [FeFe]-hydrogenases
Gustav Berggren,Gustav Berggren,Gustav Berggren,Agnieszka Adamska,Camilla Lambertz,Trevor R. Simmons,Julian Esselborn,Mohamed G. Atta,Serge Gambarelli,Jean-Marie Mouesca,Eduard J. Reijerse,Wolfgang Lubitz,Thomas Happe,Vincent Artero,Marc Fontecave,Marc Fontecave +15 more
TL;DR: It is shown that three synthetic mimics (containing different bridging dithiolate ligands) can be loaded onto bacterial Thermotoga maritima HydF and then transferred to apo-HydA1, one of the hydrogenases of Chlamydomonas reinhardtii algae, providing new mechanistic and structural insight into hydrogenase maturation.
Journal ArticleDOI
Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic
Julian Esselborn,Camilla Lambertz,Agnieszka Adamska-Venkatesh,Trevor R. Simmons,Gustav Berggren,Gustav Berggren,Jens Noth,Judith F. Siebel,Anja Hemschemeier,Vincent Artero,Edward J. Reijerse,Marc Fontecave,Marc Fontecave,Wolfgang Lubitz,Thomas Happe +14 more
TL;DR: It is shown that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins, and will be a powerful tool for developing new artificial H₂-producing catalysts.
Journal ArticleDOI
A structural view of synthetic cofactor integration into [FeFe]-hydrogenases.
Julian Esselborn,Norifumi Muraki,Kathrin Klein,Vera Engelbrecht,Nils Metzler-Nolte,Ulf-Peter Apfel,Eckhard Hofmann,Genji Kurisu,Thomas Happe +8 more
TL;DR: Crystal structures of semisynthetic [FeFe]-hydrogenases with variations in the [2Fe] cluster show little structural differences despite strong effects on activity.
Journal ArticleDOI
Molecular basis of [FeFe]-hydrogenase function: An insight into the complex interplay between protein and catalytic cofactor
TL;DR: This article summarizes, compares and categorizes the results of recent investigations based on site directed and random mutagenesis according to their informative value about structure function relationships in [FeFe]-hydrogenases.
Journal ArticleDOI
Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases
Martin Winkler,Moritz Senger,Jifu Duan,Julian Esselborn,Florian Wittkamp,Eckhard Hofmann,Ulf-Peter Apfel,Sven T. Stripp,Thomas Happe +8 more
TL;DR: Site-directed manipulation, targeting either the proton-transfer pathway or the adt ligand, significantly enhances Hhyd accumulation independent of pH, and selectively enrich the equilibrium concentration of Hhyd, applying Le Chatelier’s principle.