Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Jay P. Stasser"'
Publikováno v:
Biochemistry. 44:3143-3152
Cysteine-to-serine mutants of a maltose binding protein fusion with the human copper chaperone for superoxide dismutase (hCCS) were studied with respect to (i) their ability to transfer Cu to E,Zn superoxide dismutase (SOD) and (ii) their Zn and Cu b
Autor:
Robert J. Cotter, Christopher D. Incarvito, Pierre Moënne-Loccoz, Arnold L. Rheingold, Reza A. Ghiladi, Hong Wei Huang, Amina S. Woods, Jay P. Stasser, Kenneth D. Karlin, Ninian J. Blackburn
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 10:63-77
In the further development and understanding of heme-copper dioxygen reactivity relevant to cytochrome c oxidase O(2)-reduction chemistry, we describe a high-spin, five-coordinate dioxygen (peroxo) adduct of an iron(II)-copper(I) complex, [((6)L)Fe(I
Autor:
Nicole M. Okeley, Wilfred A. van der Donk, Moushumi Paul, Jay P. Stasser, Ninian J. Blackburn
Publikováno v:
Biochemistry. 42:13613-13624
Lantibiotics are peptide-derived antimicrobial agents that are ribosomally synthesized and posttranslationally modified by a multienzyme complex to their biologically active forms. Nisin has attracted much attention recently due to its novel mechanis
Publikováno v:
Biochemistry. 46(42)
Copper binding and X-ray aborption spectroscopy studies are reported on untagged human CCS (hCCS; CCS = copper chaperone for superoxide dismutase) isolated using an intein self-cleaving vector and on single and double Cys to Ala mutants of the hCCS M
Publikováno v:
Biochemistry. 39(25)
Copper binding to the human copper chaperone for superoxide dismutase (hCCS) has been investigated by X-ray absorption spectroscopy. Stoichiometry measurements on the dialyzed, as-isolated protein indicated that up to 3.5 Cu ions bound per hCCS molec
Autor:
Martina Ralle, Jay P. Stasser, Jack H. Kaplan, Svetlana Lutsenko, Ninian J. Blackburn, John F. Eisses
Publikováno v:
Journal of Inorganic Biochemistry. 96:43