Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Peter A. Janick"'
Autor:
David M. Yousem, Norman J. Beauchamp, Gautam Agrawal, Michelle Bittle, C. Craig Blackmore, Martin Bledsoe, John A. Bonavita, Robert F. Carfagno, Felix S. Chew, Dennis Condon, Audrey Drossner, James B. Gantenberg, Bob Gayler, Peter Ghavami, Joel A. Gross, Robin A.J. Hunt, Christopher J. Hurt, Peter A. Janick, Gregory L. Katzman, Jeffrey C. Langdon, Christopher Laubenthal, Frank James Lexa, Andrew W. Litt, F.A. Mann, Joseph Marotta, Satoshi Minoshima, Julie A. Muroff, Annemarie Relyea-Chew, Joseph Robinson, William P. Shuman
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9d9c8d1bb86bfd3da2ddd3ac91566f3
https://doi.org/10.1016/b978-032304452-3.10030-8
https://doi.org/10.1016/b978-032304452-3.10030-8
Publikováno v:
Biochemistry. 24:7942-7947
We have employed electron-nuclear double resonance (ENDOR) spectroscopy to study the bridged siroheme--[Fe4S4] cluster that forms the catalytically active center of the oxidized hemoprotein subunit (SiRo) of Escherichia coli NADPH-sulfite reductase.
Publikováno v:
Journal of Biological Chemistry. 256:2098-2101
Escherichia coli NADPH-sulfite reductase is a complex hemoflavoprotein with an alpha 8 beta 4 subunit structure. The beta-subunits each contain one siroheme and a tetranuclear iron-sulfur center (Fe4S4). Isolated beta-monomers can catalyze the 6-elec
Autor:
John C. Salerno, T A Kent, Peter A. Janick, Jodie A. Christner, Eckard Muenck, Lewis M. Siegel
Publikováno v:
Journal of the American Chemical Society. 106:6786-6794
Publikováno v:
Biochemistry. 22:5048-5054
Autor:
Lewis M. Siegel, Peter A. Janick
Publikováno v:
Biochemistry. 21:3538-3547
The hemoprotein subunit (SiR-HP) of Escherichia coli NADPH-sulfite reductase contains one siroheme (high-spin Fe3+, D = 8 cm-1) and one oxidized Fe4S4 center per polypeptide. Christner et al. [Christner, J.A., Munck, E., Janick, P.A., & Siegel, L.M.
Publikováno v:
Biochemistry. 25:4647-4654
We have employed electron-nuclear double resonance (ENDOR) spectroscopy to study the 57Fe hyperfine interactions in the bridged-siroheme [4Fe-4S] cluster that forms the catalytically active center of the two-electron-reduced hemoprotein subunit of Es
Autor:
Lewis M. Siegel, Peter A. Janick
Publikováno v:
Biochemistry. 22:504-515
Janick & Siegel [Janick, P. A., & Siegel, L. M. (1982) Biochemistry 21, 3538-3547] showed that the EPR spectrum of the reduced Fe4S4 center (S = 1/2) in fully reduced native ("unligated") Escherichia coli NADPH-sulfite reductase hemoprotein subunit (
Publikováno v:
Journal of Biological Chemistry. 258:11147-11156
We have studied the hemoprotein subunit (SiR) of Escherichia coli NADPH-sulfite reductase with Mossbauer spectroscopy in a variety of complexes and oxidation states. We demonstrated earlier for oxidized SiR (Christner, J. A., Munck, E., Janick, P. A.