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pro vyhledávání: '"35"'
Autor:
Dassama LM; Departments of †Chemistry and ‡Biochemistry and Molecular Biology, The Pennsylvania State University , University Park, Pennsylvania 16802, United States., Silakov A, Krest CM, Calixto JC, Krebs C, Bollinger JM Jr, Green MT
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2013 Nov 13; Vol. 135 (45), pp. 16758-61. Date of Electronic Publication: 2013 Oct 31.
Autor:
Dassama, Laura M. K.1,2, Silakov, Alexey1, Krest, Courtney M.1, Calixto, Julio C.1, Krebs, Carsten1,2 ckrebs@psu.edu, Martin Bollinger Jr., J.1,2 jmb21@psu.edu, Green, Michael T.1 mtg10@psu.edu
Publikováno v:
Journal of the American Chemical Society. 11/13/2013, Vol. 135 Issue 45, p16758-16761. 4p.
Autor:
Julio C. Calixto, Michael Green, Laura M. K. Dassama, J. Martin Bollinger, Alexey Silakov, Courtney M. Krest, Carsten Krebs
Publikováno v:
Journal of the American Chemical Society. 135(45)
A class Ia ribonucleotide reductase (RNR) employs a μ-oxo-Fe2(III/III)/tyrosyl radical cofactor in its β subunit to oxidize a cysteine residue ~35 A away in its α subunit; the resultant cysteine radical initiates substrate reduction. During self-a
Publikováno v:
Journal of the American Chemical Society. 131(9)
We previously used a combination of CW and pulsed-ENDOR protocols to identify the types of protonated oxygen (OHx) species and their disposition within the FeIII/FeIV cluster of Intermediate X, the direct precursor of the essential diferric-tyrosyl r