Zobrazeno 1 - 10
of 109
pro vyhledávání: '"Joseph Kraut"'
Autor:
Jesus E. Villafranca, Elizabeth E. Howell, Donald H. Voet, Marjorie S. Strobel, Richard C. Ogden, John N. Abelson, Joseph Kraut
Publikováno v:
Biotechnology & Biological Frontiers ISBN: 9780429050329
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::054bbf9971013ec45dea103f788af6fc
https://doi.org/10.4324/9780429050329-33
https://doi.org/10.4324/9780429050329-33
Publikováno v:
Biochemistry. 35:12742-12761
Mammalian DNA polymerase beta (pol beta) is a small (39 kDa) DNA gap-filling enzyme that comprises an amino-terminal 8-kDa domain and a carboxy-terminal 31-kDa domain. In the work reported here, crystal structures of human pol beta complexed with blu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f716b0853b1aac74537a5301f77eb580
https://doi.org/10.1021/bi952955d
https://doi.org/10.1021/bi952955d
Publikováno v:
Biochemistry. 34:2710-2723
Crystal structures of Escherichia coli dihydrofolate reductase (ecDHFR, EC 1.5.1.3) in binary complexes with folate, 5-deazafolate (5dfol), and 5,10-dideazatetrahydrofolate (ddTHF) have been refined to R-factors of 13.7%, 14.9%, and 14.5%, respective
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29ad7eded78b58b92e4ef9c341c449c9
https://doi.org/10.1021/bi00008a039
https://doi.org/10.1021/bi00008a039
Publikováno v:
Nature Structural Biology. 1:524-531
The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b897b7b2e401378be67012a22a5a928a
https://doi.org/10.1038/nsb0894-524
https://doi.org/10.1038/nsb0894-524
Publikováno v:
Science. 264:1891-1903
Two ternary complexes of rat DNA polymerase beta (pol beta), a DNA template-primer, and dideoxycytidine triphosphate (ddCTP) have been determined at 2.9 A and 3.6 A resolution, respectively. ddCTP is the triphosphate of dideoxycytidine (ddC), a nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4838cf558615926993d87ceea3e25362
https://doi.org/10.1126/science.7516580
https://doi.org/10.1126/science.7516580
Publikováno v:
Science. 264:1930-1935
Structures of the 31-kilodalton catalytic domain of rat DNA polymerase beta (pol beta) and the whole 39-kilodalton enzyme were determined at 2.3 and 3.6 angstrom resolution, respectively. The 31-kilodalton domain is composed of fingers, palm, and thu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::256ebbdc7c746cf6bbdf554396b3962d
https://doi.org/10.1126/science.7516581
https://doi.org/10.1126/science.7516581
Publikováno v:
Biochemistry. 33:1473-1480
The reactions of recombinant cytochrome c peroxidase [CcP(MI)] and a number of CcP(MI) mutants with native and ruthenium-labeled horse ferrocytochrome c have been studied by stopped-flow spectroscopy and laser flash photolysis. At 100 mM ionic streng
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ffd5305574f48518352876748e3fe7d
https://doi.org/10.1021/bi00172a025
https://doi.org/10.1021/bi00172a025
Autor:
Huguette Pelletier, Joseph Kraut
Publikováno v:
Science. 258:1748-1755
The crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c was determined at 2.3 A resolution. This structure reveals a possible electron transfer pathway unlike any previously proposed for this extensiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b70f21f78bccc1862008c1d4d4c09f5
https://doi.org/10.1126/science.1334573
https://doi.org/10.1126/science.1334573
Publikováno v:
Biochemistry. 31:11524-11535
The spectroscopic properties of a mutant cytochrome c peroxidase, in which Asp-235 has been replaced by an asparagine residue, were examined in both nitrate and phosphate buffers between pH 4 and 10.5. The spin state of the enzyme is pH dependent, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28a8b16f1b63c6f09847de00ae1b2bf9
https://doi.org/10.1021/bi00161a034
https://doi.org/10.1021/bi00161a034
Autor:
Douglas Magde, John T. Hirai, Martin F. Farnum, Janet K. Grimsley, Elizabeth E. Howell, Mark S. Warren, Joseph Kraut
Publikováno v:
Biochemistry. 30:11567-11579
A remarkable correlation has been discovered between fluorescence lifetimes of bound NADPH and rates of hydride transfer among mutants of dihydrofolate reductase (DHFR) from Escherichia coli. Rates of hydride transfer from NADPH to dihydrofolate chan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba6eba405c9bbda4c16dfa699ddfe8dc
https://doi.org/10.1021/bi00113a012
https://doi.org/10.1021/bi00113a012