Zobrazeno 1 - 10
of 637
pro vyhledávání: '"J, Koebke"'
Autor:
Ayesha M. Patel, Karl J. Koebke, Timothy J. Grunkemeyer, Colleen M. Riordan, Youngsoo Kim, Ryan C. Bailey, E. Neil G. Marsh
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-8 (2022)
Abstract Viperin is a radical S-adenosylmethionine enzyme that catalyzes the formation of the antiviral ribonucleotide, 3’-deoxy-3’,4’-didehydroCTP. The enzyme is conserved across all kingdoms of life, and in higher animals viperin is localized
Externí odkaz:
https://doaj.org/article/bf20f6509eeb4dff83e8abb04e467a1d
Publikováno v:
Chemical Reviews. 122:12046-12109
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0908b7534df647b8f93dbe5ea2b1279c
https://doi.org/10.1021/acs.chemrev.1c01025
https://doi.org/10.1021/acs.chemrev.1c01025
Publikováno v:
Frontiers in Molecular Biosciences, Vol 6 (2019)
The design of metal-binding sites in proteins that combine high affinity with high selectivity for the desired metal ion remains a challenging goal. Recently, a protein designed to display femtomolar affinity for UO22+, dubbed “Super Uranyl-binding
Externí odkaz:
https://doaj.org/article/f786cc78ea5d4079bc60a8d8db5374ed
Autor:
Aathmaja Anandhi Rangarajan, Karl J. Koebke, E. Neil G. Marsh, Nicole M. Koropatkin, Hannah E. Chia, Julie S. Biteen
Publikováno v:
ACS Chemical Biology. 16:2109-2115
Bilin-binding fluorescent proteins like UnaG-bilirubin are noncovalent ligand-dependent reporters for oxygen-free microscopy but are restricted to blue and far-red fluorescence. Here we describe a high-throughput screening approach to provide a new U
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38b5ec723578b137c8c21394f7b15f0a
https://doi.org/10.1021/acschembio.1c00391
https://doi.org/10.1021/acschembio.1c00391
Autor:
James E. Penner-Hahn, Vincent L. Pecoraro, Elizabeth C. Manickas, Karl J. Koebke, Alison G. Tebo, Aniruddha Deb
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 26:855-862
Copper nitrite reductase (CuNiR) is a copper enzyme that converts nitrite to nitric oxide and is an important part of the global nitrogen cycle in bacteria. The relatively simple CuHis3 binding site of the CuNiR active site has made it an enticing ta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9b9b0ee65212efa0c1362ba2cd8d35b
https://doi.org/10.1007/s00775-021-01889-1
https://doi.org/10.1007/s00775-021-01889-1
Autor:
Anabella Ivancich, Olga Iranzo, Elisabeth Lojou, Barbara Schoepp-Cothenet, Karl J. Koebke, Borries Demeler, Vincent L. Pecoraro, Toni Kühl
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angew Chem Int Ed Engl
Angewandte Chemie International Edition, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angew Chem Int Ed Engl
Angewandte Chemie International Edition, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
International audience; De Novo metalloprotein design assesses the relationship between metal active site architecture and catalytic reactivity. Herein, we use an alpha-helical scaffold to control the iron coordination geometry when a heme cofactor i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::075e26d97a85efd80fb3eb738b10f55c
https://doi.org/10.1002/ange.202012673
https://doi.org/10.1002/ange.202012673
Publikováno v:
Angewandte Chemie. 132:7750-7773
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e8281f25d88329d4f5b218567dfbedf
https://doi.org/10.1002/ange.201907502
https://doi.org/10.1002/ange.201907502
Autor:
Audrey E. Tolbert, Emilie Mathieu, Vincent L. Pecoraro, James E. Penner-Hahn, Cédric Tard, Clotilde Policar, Karl J. Koebke, Olga Iranzo
Publikováno v:
Chemistry-A European Journal
Chemistry-A European Journal, Wiley-VCH Verlag, 2020, 26 (1), pp.249-258. ⟨10.1002/chem.201903808⟩
Chemistry
Chemistry-A European Journal, 2020, 26 (1), pp.249-258. ⟨10.1002/chem.201903808⟩
Chemistry-A European Journal, Wiley-VCH Verlag, 2020, 26 (1), pp.249-258. ⟨10.1002/chem.201903808⟩
Chemistry
Chemistry-A European Journal, 2020, 26 (1), pp.249-258. ⟨10.1002/chem.201903808⟩
Superoxide dismutases (SODs) are highly efficient enzymes for superoxide dismutation and the first line of defense against oxidative stress. These metalloproteins contain a redox-active metal ion in their active site (Mn, Cu, Fe, Ni) with a tightly c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afa78986f8bd186c8bfc9eb6d162b3ff
https://doi.org/10.1002/chem.201903808
https://doi.org/10.1002/chem.201903808
Autor:
Karl J. Koebke, Wen Guo, Tieyi Lu, Xingquan Zou, Tao Wei, Zhan Chen, E. Neil G. Marsh, Marie Hoarau, Ralph Crisci, Hanjie Jiang
Publikováno v:
The journal of physical chemistry. B. 125(28)
Recently, a super uranyl binding protein (SUP) was developed, which exhibits excellent sensitivity/selectivity to bind uranyl ions. It can be immobilized onto a surface in sensing devices to detect uranyl ions. Here, sum frequency generation (SFG) vi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a52bd5bdc28f3e158ac09680b74e9a55
https://pubmed.ncbi.nlm.nih.gov/34254804
https://pubmed.ncbi.nlm.nih.gov/34254804
Noncoded Amino Acids in de Novo Metalloprotein Design: Controlling Coordination Number and Catalysis
Autor:
Karl J. Koebke, Vincent L. Pecoraro
Publikováno v:
Accounts of Chemical Research. 52:1160-1167
The relationship between structure and function has long been one of the major points of investigation in Biophysics. Understanding how much, or how little, of a protein’s often complicated structure is necessary for its function can lead to direct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9747947bf871fc8220c0e60d40e6aa1a
https://doi.org/10.1021/acs.accounts.9b00032
https://doi.org/10.1021/acs.accounts.9b00032