Výsledky vyhledávání - "Jae‐Hun Jeoung"

Akademický článek

Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy.

Autor: Peer Schrapers, Julia Ilina, Christina M Gregg, Stefan Mebs, Jae-Hun Jeoung, Holger Dau, Holger Dobbek, Michael Haumann

Publikováno v: PLoS ONE, Vol 12, Iss 2, p e0171039 (2017)

Bacteria integrate CO2 reduction and acetyl coenzyme-A (CoA) synthesis in the Wood-Ljungdal pathway. The acetyl-CoA synthase (ACS) active site is a [4Fe4S]-[NiNi] complex (A-cluster). The dinickel site structure (with proximal, p, and distal, d, ions

Externí odkaz: https://doaj.org/article/703ef1f0bf3845a4862a5bf790ef31d5

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Akademický článek

Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis

Autor: Lei Peng, Aysu Yarman, Katharina J. Jetzschmann, Jae-Hun Jeoung, Daniel Schad, Holger Dobbek, Ulla Wollenberger, Frieder W. Scheller

Publikováno v: Sensors, Vol 16, Iss 3, p 272 (2016)

For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein

Externí odkaz: https://doaj.org/article/d52465e4e0b84cf58c961c8d0c3f4a52

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Structural basis for coupled ATP-driven electron transfer in the double-cubane cluster protein

Autor: Jae-Hun Jeoung, Sabine Nicklisch, Holger Dobbek

Publikováno v: Proceedings of the National Academy of Sciences. 119

Electron transfers coupled to the hydrolysis of ATP allow various metalloenzymes to catalyze reductions at very negative reduction potentials. The double-cubane cluster protein (DCCP) catalyzes the reduction of small molecules, such as acetylene and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d57cb8e7863de638cae2be3242ae37c0
https://doi.org/10.1073/pnas.2203576119

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A Morphing [4Fe-3S-nO]-Cluster within a Carbon Monoxide Dehydrogenase Scaffold

Autor: Jae‐Hun Jeoung, Jochen Fesseler, Lilith Domnik, Friederike Klemke, Malte Sinnreich, Christian Teutloff, Holger Dobbek

Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) catalyze the reversible reduction of CO2 to CO. Several anaerobic microorganisms encode multiple CODHs in their genome, of which some, despite being annotated as CODHs, lack a cysteine of the ca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe9335f92e0afa221e643e03422533da
http://edoc.hu-berlin.de/18452/26813

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Determining the oxidation state of elements by X ray crystallography

Autor: Frank Lennartz, Jae-Hun Jeoung, Stefan Ruenger, Holger Dobbek, Manfred S. Weiss

Protein-mediated redox reactions play a critical role in many biological processes and often occur at centres that contain metal ions as cofactors. In order to understand the exact mechanisms behind these reactions it is important to not only charact

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89633e7646aa2d4b9415106860b60ea5
http://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=107403

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Bimetallic Mn, Fe, Co, and Ni Sites in a Four-Helix Bundle Protein: Metal Binding, Structure, and Peroxide Activation

Autor: Holger Dobbek, Anna Fischer, Holger Dau, Michael Haumann, Ulla Wollenberger, Friederike Klemke, Stefan Rünger, Jae-Hun Jeoung, Bettina Neumann, Victoria Davis

Publikováno v: Inorganic chemistry. 60(23)

Bimetallic active sites in enzymes catalyze small-molecule conversions that are among the top 10 challenges in chemistry. As different metal cofactors are typically incorporated in varying protein scaffolds, it is demanding to disentangle the individ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::471a6582a24349eb8f009c8f21d307b0
https://pubmed.ncbi.nlm.nih.gov/34757735

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