Zobrazeno 1 - 10
of 12
pro vyhledávání: '"35"'
Autor:
R. Adam Kinney, Bo Zhang, Rebecca L. McNaughton, Russ Hille, Muralidharan Shanmugam, Brian M. Hoffman
Publikováno v:
Journal of the American Chemical Society. 132:14015-14017
The formaldehyde-inhibited Mo(V) state of xanthine oxidase (I) has been studied for four decades, yet it has not proven possible to distinguish unequivocally among the several structures proposed for this form. The uniquely large isotropic hyperfine
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
Publikováno v:
Journal of the American Chemical Society. 123(11)
Xanthine oxidase is a molybdenum-containing enzyme that catalyzes the hydroxylation of xanthine and a wide variety of other aromatic heterocycles. In the course of the reaction with xanthine and substrates such as 2-hydroxy-6-methylpurine (HMP), the
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
Autor:
Petra Hänzelmann, Sowmya Subramanian, Michael K. Johnson, Brian M. Hoffman, Heather L. Hernandez, Hermann Schindelin, Nicholas S. Lees
Publikováno v:
Journal of the American Chemical Society. 131:9184-9185
The S-adenosylmethionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of guanosine 5'-triphosphate (5'-GTP) into precursor Z. A published X-ray crystal structure of MoaA wit
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:
Stoyan K. Smoukov, Brian M. Hoffman, Stephen J. Lippard, Daniel A. Kopp, Roman Davydov, Ann M. Valentine
Publikováno v:
Journal of the American Chemical Society. 124:2657-2663
The binding of ethanol and 1,1,1-trifluoroethanol (TFE) to both the H(mv) and H(ox) forms of soluble methane monooxygenase (sMMO) in solution has been studied by Q-band (35 GHz) CW and pulsed ENDOR spectroscopy of (1)H, (2)H and (19)F nuclei of exoge
Publikováno v:
Journal of the American Chemical Society. 132(43)
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides and requires a diferric-tyrosyl radical (Y(•)) cofactor to initiate catalysis. The initiation process requires long-rang
Autor:
Robert G. Griffin, Sylwia Kacprzak, Brian Hoffman, Erin Artin, JoAnne Stubbe, Hendrik Zipse, Debora Marcela Martino, Nicholas Lees, Martin Kaupp, Gregory J. S. Lohman, Marina Bennati, Stanislaw F. Wnuk
Publikováno v:
Journal of the American Chemical Society
The Escherichia coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleoside diphosphates to deoxynucleotides and requires a diferric-tyrosyl radical cofactor for catalysis. RNR is composed of a 1:1 complex of two homodimeric subunits: