Zobrazeno 1 - 10
of 13
pro vyhledávání: '"35"'
Publikováno v:
Journal of the American Chemical Society. 125:11379-11384
Interdomain motions of Ca(2+)-ligated calmodulin were characterized by analyzing the nuclear magnetic resonance (15)N longitudinal relaxation rate R(1), transverse relaxation rate R(2), and steady-state {(1)H}-(15)N NOE of the backbone amide group at
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
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. 119:12192-12200
The two available crystallographic structures of cobalamin dependent enzymes, the 27 kDa fragment of the methylcobalamin-dependent enzyme, methionine synthase, from Escherichia coli [Drennan, C. L. et al. Science 1994, 266, 1669] and the 5‘-deoxyad
Publikováno v:
Journal of the American Chemical Society. 119:10121-10126
The resting state of nitrogenase shows an S = 3/2 electron paramagnetic resonance (EPR) signal resulting from the FeMo-cofactor (MoFe7S9:homocitrate) of the MoFe protein. When the enzyme undergoes turnover under a CO atmosphere, this signal disappear
Publikováno v:
Journal of the American Chemical Society. 117:11619-11627
The detailed mechanism of DNA hydrolysis by enzymes is of significant current interest. One of the most important questions in this respect is the catalytic role of metal ions such as Mg{sup 2+}. Experimental evaluation of the catalytic effects of th
Publikováno v:
Journal of the American Chemical Society. 131(3)
Unlike most ordered molecular systems, globular proteins exhibit a temperature of maximum stability, implying that the structure can be disrupted by cooling. This cold denaturation phenomenon is usually linked to the temperature-dependent hydrophobic
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:
Allen M. Orville, Jeffrey M. Zaleski, Edward I. Solomon, Mindy I. Davis, Frank Neese, John D. Lipscomb
Publikováno v:
Journal of the American Chemical Society. 124(4)
The geometric and electronic structure of the high-spin ferric active site of protocatechuate 3,4-dioxygenase (3,4-PCD) has been examined by absorption (Abs), circular dichroism (CD), magnetic CD (MCD), and variable-temperature-variable-field (VTVH)