Zobrazeno 1 - 10
of 43
pro vyhledávání: '"John P. Caradonna"'
Autor:
Joshua S. McNally, Patrick J. Cappillino, Matthew D. Krzyaniak, Michael Howart, John P. Caradonna, John McCracken, Paul C. Tarves
Publikováno v:
Inorganic Chemistry. 54:6486-6497
Electron paramagnetic resonance (EPR) experiments were done on a series of S = (3)/2 ferrous nitrosyl model complexes prepared with chelating ligands that mimic the 2-His-1-carboxylate facial triad iron binding motif of the mononuclear nonheme iron o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f8eea8b424960b7da2a26dcbe32918c
https://doi.org/10.1021/acs.inorgchem.5b00788
https://doi.org/10.1021/acs.inorgchem.5b00788
Publikováno v:
Dalton Trans.. 41:474-483
Mononuclear nonheme iron oxygenase (MNO) enzymes contain a subclass of metalloproteins capable of catalyzing the O(2)-dependent hydroxylation of unactivated substrates at a ferrous ion center coordinated to a highly conserved His-His-Glu/Asp motif. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c1ee448a2752bdb3c067ba97699bc85
https://doi.org/10.1039/c1dt11199j
https://doi.org/10.1039/c1dt11199j
Autor:
John R. Miecznikowski, George P. Lisi, Anthony M. Martinez, Kathleen M. Foley, John P. Caradonna, Daniel J. Kwiecien
Publikováno v:
Journal of Chemical Education. 88:657-661
A three-week laboratory experiment, which introduces students in an advanced inorganic chemistry course to air-sensitive chemistry and catalysis, is described. During the first week, the students synthesize RuCl2(PPh3)3. During the second and third w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0dfa3bc6224d80764cb99791253054a
https://doi.org/10.1021/ed1001575
https://doi.org/10.1021/ed1001575
Autor:
Paul C. Tarves, Corina Rogge, Wayne Lo, Gerard T. Rowe, Patrick J. Cappillino, William H. Armstrong, Andrew J. Lewis, Mark Harvey, John P. Caradonna, Adonis Stassinopoulos
Publikováno v:
Inorganica Chimica Acta. 362:2136-2150
A series of binuclear iron compounds has been synthesized using diamide, bis-phenolate ligands in which the carbon-linker between the amide nitrogen atoms has been varied. Two diferrous compounds in the series, Fe 2 II ( H 2 Hbach ) 2 ( N-MeIM ) 2 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b88a8cdd2d0ee61b57e584a7bfc1b7f3
https://doi.org/10.1016/j.ica.2008.09.036
https://doi.org/10.1016/j.ica.2008.09.036
Autor:
Keith O. Hodgson, Britt Hedman, John P. Caradonna, Edward I. Solomon, Nataša Mitić, Erik C. Wasinger
Publikováno v:
Biochemistry. 41:6211-6217
Previous studies of ferrous wild-type phenylalanine hydroxylase, [Fe(2+)]PAH(T)[], have shown the active site to be a six-coordinate distorted octahedral site. After the substrate and cofactor bind to the enzyme ([Fe(2+)]PAH(R)[L-Phe,5-deaza-6-MPH(4)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a2699dae4ec51708e1152c9d79c17d6
https://doi.org/10.1021/bi0121510
https://doi.org/10.1021/bi0121510
Publikováno v:
Inorganica Chimica Acta. 297:313-329
The reaction of Co2+(N-MeIm)2(Cl)2 (1), with Li2H2Hbab (H4Hbab=1,2-bis(2-hydroxybenzamido)benzene) affords the binuclear complex [Co2 2+(H2Hbab)2(N-MeIm)2] (2). Single crystal X-ray crystallography shows that the two Co2+ centers in 2 are related by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e66a5761d2f86989e77d408b337437ad
https://doi.org/10.1016/s0020-1693(99)00431-4
https://doi.org/10.1016/s0020-1693(99)00431-4
Autor:
Jyllian N. Kemsley, Kelly Loeb Zaleski, Edward I. Solomon, John P. Caradonna,§ and, Nataša Mitić
Publikováno v:
Journal of the American Chemical Society. 121:1528-1536
The tetrahydrobiopterin-dependent enzyme phenylalanine hydroxylase (PAH) contains one non-heme iron atom per subunit that is required for reactivity. We have applied circular dichroism (CD), magnetic circular dichroism (MCD), and variable-temperature
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f5c82786b17875337eddeab0d5d9834
https://doi.org/10.1021/ja9833063
https://doi.org/10.1021/ja9833063
Publikováno v:
Proceedings of the National Academy of Sciences. 94:6635-6640
Rational protein design is an emerging approach for testing general theories of protein chemistry through the creation of new structures and functions. Here we present the first successful introduction by rational design of a [Fe 4 S 4 ] cuboidal clu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e310aca7244a1db8be1ea058a774c4bd
https://doi.org/10.1073/pnas.94.13.6635
https://doi.org/10.1073/pnas.94.13.6635
Publikováno v:
Proceedings of the National Academy of Sciences. 94:5562-5567
The rational protein design algorithm DEZYMER was used to introduce the active site of nonheme iron superoxide dismutase (SOD) into the hydrophobic interior of the host protein, Escherichia coli thioredoxin (Trx), a protein that does not naturally co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19e05ff133a65c72643ceef428c712cb
https://doi.org/10.1073/pnas.94.11.5562
https://doi.org/10.1073/pnas.94.11.5562
Publikováno v:
Journal of Biological Chemistry. 272:7801-7809
The carboxyl terminus of transcription factor Sp1 contains three contiguous Cys2-His2 zinc finger domains with the consensus sequence Cys-X2-4-Cys-X12-His-X3-His. We have used standard homonuclear two-dimensional NMR techniques to solve the solution
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d16819760959a3df9774e82aaacca54
https://doi.org/10.1074/jbc.272.12.7801
https://doi.org/10.1074/jbc.272.12.7801