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pro vyhledávání: '"35"'
Autor:
Jeremy M. Smith, Brian M. Hoffman, Martin L. Kirk, Benjamin W. Stein, Deepak Subedi, George E. Cutsail
Publikováno v:
Journal of the American Chemical Society
The recently synthesized and isolated low-coordinate Fe(V) nitride complex has numerous implications as a model for high-oxidation states in biological and industrial systems. The trigonal [PhB((t)BuIm)3Fe(V)≡N](+) (where (PhB((t)BuIm)3(-) = phenyl
Autor:
Mohammad R. Seyedsayamdost, Tomislav Argirević, JoAnne Stubbe, Ellen Catherine Minnihan, Marina Bennati
Publikováno v:
Journal of the American Chemical Society
E. coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides, a process that requires long-range radical transfer over 35 A from a tyrosyl radical (Y(122)*) within the beta2 subunit to a cysteine residue (C(439))
Autor:
Somdatta Ghosh, Abhishek Dey, Charles P. Scholes, Vladimir M. Grigoryants, Edward I. Solomon, Oleg M. Usov, Yan Sun
Publikováno v:
Journal of the American Chemical Society. 129(34)
Copper nitrite reductase (NiR) is a homotrimeric enzyme, containing a T1 copper site, which transfers electrons to the T2 catalytic site, where nitrite is reduced by one electron to nitric oxide (NO2− + 2H+ + e− → NO + H2O).1–3 Recently a sid
Publikováno v:
Journal of the American Chemical Society. 127(23)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, which contains a phosphonate group. The active site of this enzyme consists of a high-spin Mn(2+) ion coordinated by endogenous li
Autor:
William E. Broderick, Brian M. Hoffman, Joan B. Broderick, Charles J. Walsby, Jennifer Cheek, Danilo Ortillo, Wei Hong
Publikováno v:
Journal of the American Chemical Society. 124(12)
Pyruvate formate-lyase activating enzyme (PFL-AE) is a representative member of an emerging family of enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (AdoMet) to initiate radical catalysis. Although these enzymes have diverse funct
Publikováno v:
Journal of the American Chemical Society. 132:2526-2527
We here report the first direct evidence addressing the possible involvement of Mo in substrate interactions during catalytic turnover. When the alpha-70(Ile) MoFe protein is freeze-trapped during H(+) reduction under Ar, the majority of the resting