Zobrazeno 1 - 7 of 7 pro vyhledávání: '"Jean-Paul Willems"'
1
The Core Structure of X Generated in the Assembly of the Diiron Cluster of Ribonucleotide Reductase: 17O2 and H217O ENDOR
Autor: JoAnne Stubbe, Doug Burdi, William E. Antholine, Brian M. Hoffman, Pam Riggs-Gelasco, Jean Paul Willems
Publikováno v: Journal of the American Chemical Society. 120:12910-12919
The intermediate, designated X, formed during the self-assembly reaction of the tyrosyl radical/μ-oxo-bridged diferric cofactor in the R2 subunit of Escherichia coli ribonucleotide reductase (RNR) is directly involved in the oxidation of Y122 to the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::09f2c9de67c8cee7053781941bc7752b
https://doi.org/10.1021/ja9824270
Zobrazit plný text záznamu
2
Small Molecule Binding to the Mixed-Valent Diiron Center of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath) as Revealed by ENDOR Spectroscopy
Autor: Ann M. Valentine, Brian M. Hoffman, Stephen J. Lippard, Jean Paul Willems, Ryszard J. Gurbiel
Publikováno v: Journal of the American Chemical Society. 120:9410-9416
The binding of several exogenous molecules at the active site of the soluble methane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) is described. The interaction of methanol, the product of methane hydroxylation, with the mixed
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1ca9fd9a62d9ea8fa49501b988c48d19
https://doi.org/10.1021/ja980795y
Zobrazit plný text záznamu
3
High-Frequency EPR and Pulsed Q-Band ENDOR Studies on the Origin of the Hydrogen Bond in Tyrosyl Radicals of Ribonucleotide Reductase R2 Proteins from Mouse and Herpes Simplex Virus Type 1
Autor: Astrid Gräslund, Pieter J. van Dam, Stephan Pötsch, Anne Laure Barra, K. Kristoffer Andersson, Peter P. Schmidt, Brian M. Hoffman, Jean Paul Willems, Wilfred R. Hagen
Publikováno v: Journal of the American Chemical Society. 120:5080-5085
The g tensor of the tyrosyl radical present in the active R2 protein of ribonucleotide reductase is anisotropic, and the g1 component is influenced by hydrogen bonding to the oxygen of the tyrosyl ...
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c0b0a11fa668400784f7a1c1848c59ee
https://doi.org/10.1021/ja9737127
Zobrazit plný text záznamu
4
Identification of the Protonated Oxygenic Ligands of Ribonucleotide Reductase Intermediate X by Q-Band 1,2H CW and Pulsed ENDOR
Autor: Hong-In Lee, JoAnne Stubbe,⊥ and, Doug Burdi, † Jean-Paul Willems, Brian M. Hoffman, Peter E. Doan
Publikováno v: Journal of the American Chemical Society. 119:9816-9824
We report CW and pulsed Q-band 1,2H ENDOR measurements of intermediate X formed during the assembly of the diferric tyrosyl radical cofactor of the R2 subunit in ribonucleotide reductase. These studies, performed with H2O and D2O buffers, were design
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e50bc16175b593a57617edcc415076d0
https://doi.org/10.1021/ja9709942
Zobrazit plný text záznamu
5
Electron Paramagnetic Resonance Investigations of a Kinetically Competent Intermediate Formed in Ribonucleotide Reduction: Evidence for a Thiyl Radical-Cob(II)alamin Interaction
Autor: Gary J. Gerfen, Brian M. Hoffman, Jean Paul Willems, Stuart Licht, JoAnne Stubbe
Publikováno v: Journal of the American Chemical Society. 118:8192-8197
The ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii requires adenosylcobalamin (AdoCbl) as a cofactor to catalyze the conversion of nucleotides to deoxynucleotides. RTPR has previously been shown to catalyze the homolytic
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::201693894015c84b88dff29c23fa0a7a
https://doi.org/10.1021/ja960363s
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje