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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 LM; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA., Boal AK, Krebs C, Rosenzweig AC, Bollinger JM Jr
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2012 Feb 08; Vol. 134 (5), pp. 2520-3. Date of Electronic Publication: 2012 Jan 25.
Publikováno v:
Journal of the American Chemical Society. 134:2520-2523
The reaction of a class I ribonucleotide reductase (RNR) begins when a cofactor in the β subunit oxidizes a cysteine residue ~35 Å away in the α subunit, generating a thiyl radical. In the class Ic enzyme from Chlamydia trachomatis (Ct), the cyste
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