Zobrazeno 1 - 10
of 22
pro vyhledávání: '"35"'
Autor:
Christopher M. Lauderback, David Allan Butterfield, Jaroslaw Kanski, Marina V. Aksenova, Sridhar Varadarajan
Publikováno v:
Journal of the American Chemical Society. 123(24)
Oxidative stress induced by amyloid beta-peptide (A beta) has been implicated in the neurodegeneration observed in Alzheimer's disease (AD) brain. However, the mechanism by which the predominant form of A beta found in AD brains, A beta(1--42), cause
Autor:
Bogdan Tarus, Gal Bitan, Margaret M. Condron, David B. Teplow, John E. Straub, Hilal A. Lashuel, Sabrina S. Vollers
Publikováno v:
Journal of the American Chemical Society. 125:15359-15365
Aberrant protein oligomerization is an important pathogenetic process in vivo. In Alzheimer's disease (AD), the amyloid beta-protein (Abeta) forms neurotoxic oligomers. The predominant in vivo Abeta alloforms, Abeta40 and Abeta42, have distinct oligo
Publikováno v:
J Am Chem Soc
We report an air-stable diradical dication of chiral D(2)-symmetric conjoined bis[5]diazahelicene with unprecedented high spin (triplet) ground state, singlet triplet energy gap, ΔE(ST) = 0.3 kcal mol(−1). The diradical dication possesses closed-s
Publikováno v:
Journal of the American Chemical Society. 139:16657-16665
Ribonucleotide reductases (RNR) catalyze the reduction of nucleotides to deoxynucleotides through a mechanism involving an essential cysteine based thiyl radical. In the E. coli class 1a RNR the thiyl radical (C439•) is a transient species generate
Autor:
Matthew O. Ross, Igor D. Petrik, Pierre Moënne-Loccoz, Yelu Shi, Yi Lu, Qianhong Zhu, Ambika Bhagi-Damodaran, Julian Reed, Yong Zhang, Saumen Chakraborty, Evan N. Mirts
Publikováno v:
Journal of the American Chemical Society. 139(35)
The presence of nonheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzymatic activity of reducing O2 to H2O, but the exact mechanism the nonheme metal ion uses to confer and fine-tune the activity
Autor:
Larry E. Overman, David W. C. MacMillan, Christopher C. Nawrat, Yuriy Slutskyy, Christopher R. Jamison
Publikováno v:
Journal of the American Chemical Society, vol 137, iss 35
Alkyl oxalates are new bench-stable alcohol-activating groups for radical generation under visible light photoredox conditions. Using these precursors, the first net redox-neutral coupling of tertiary and secondary alcohols with electron-deficient al
Autor:
Brian M. Hoffman, Joshua Telser, Brett M. Barney, Peter E. Doan, Lance C. Seefeldt, Robert Y. Igarashi, Dennis R. Dean
Publikováno v:
Journal of the American Chemical Society. 133:17329-17340
N(2) binds to the active-site metal cluster in the nitrogenase MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-homocitrate-X]; FeMo-co) only after the MoFe protein has accumulated three or four electrons/protons (E(3) or E(4) states), with the E(4) state
Autor:
Peter E. Doan, Patricia C. Dos Santos, Hong-In Lee, Mikhail Laryukhin, Brian M. Hoffman, Lance C. Seefeldt, Dennis R. Dean, Robert Y. Igarashi
Publikováno v:
Journal of the American Chemical Society. 126:9563-9569
Nitrogenase is the metalloenzyme that catalyzes the nucleotide-dependent reduction of N(2), as well as reduction of a variety of other triply bonded substrates, including the alkyne, acetylene. Substitution of the alpha-70(Val) residue in the nitroge
Autor:
Koichiro Ishimori, Isao Morishima, Takehiko Tosha, Shiro Yoshioka, Hiroshi Hori, Satoshi Takahashi
Publikováno v:
Journal of the American Chemical Society. 124:14571-14579
Structural and functional roles of the hydrogen bonding network that surrounds the heme-thiolate coordination of P450(cam) from Pseudomonas putida were investigated. A hydrogen bond between the side chain amide of Gln360 and the carbonyl oxygen of th
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