Zobrazeno 1 - 10
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pro vyhledávání: '"Christopher J. Kay"'
Autor:
Christopher J. Kay
Publikováno v:
FEBS Letters. 403:230-235
β-Amyloid peptides (Aβ) form the core of Alzheimer's disease (AD) senile plaques, and are implicated in AD neurotoxicity. Aβ and some derivatives generate free radicals upon fibrilogenesis. A mechanism for free radical generation is proposed, base
Publikováno v:
Biochemistry. 35:14109-14117
5-Aminolevulinate synthase catalyzes the first step of the heme biosynthetic pathway in animals, fungi, and some bacteria. The enzyme belongs to a large family of enzymes that use pyridoxal 5'-phosphate as an essential cofactor. We previously analyze
Autor:
Christopher J. Kay, Eric W. Lippay
Publikováno v:
Biochemistry. 31:11376-11382
Kinetic and thermodynamic properties of yeast flavocytochrome b2 (EC 1.1.2.3) are modified by the product pyruvate, which binds to the flavosemiquinone (FSQ) form of the prosthetic flavin and decreases the thermodynamic driving force for electron tra
Publikováno v:
Biochemistry. 30:11445-11450
Assimilatory nitrate reductase (NR) from Chlorella is homotetrameric, each subunit containing FAD, heme, and Mo-pterin in a 1:1:1 stoichiometry. Measurements of NR activity and steady-state reduction of the heme component under conditions of NADH lim
Autor:
Christopher J. Kay, Andrew C. Cannons, Charles R. Hipkin, Larry P. Solomonson, David A. Kau, Michael J. Barber
Publikováno v:
Biochemical Journal. 272:545-548
Visible spectra of oxidized and reduced Candida nitratophila assimilatory NAD(P)H:nitrate reductase yielded absorbance maxima of 413 nm and 423 nm, and 525 nm and 555 nm respectively, characteristic of a b5-type cytochrome. E.p.r. spectra of the part
Autor:
Christopher J. Kay, Michael J. Barber
Publikováno v:
Analytical Biochemistry. 184:11-15
A room temperature electron paramagnetic resonance potentiometric cell has been developed for the measurement of oxidation-reduction midpoint potentials of enzymes containing paramagnetic centers. Based upon an aqueous flat cell designed for use with
Autor:
Christopher J. Kay, Michael J. Barber
Publikováno v:
Archives of biochemistry and biophysics. 326(2)
Assimilatory NADH:nitrate reductase catalyzes the transfer of reducing equivalents from NADH to molecular oxygen. Initial rate studies performed under conditions of optimum pH (8.0) and constant ionic strength (μ = 0.2) revealed that the maximal rat
Publikováno v:
Biochemistry. 29(48)
Potentiometric titrations of assimilatory nitrate reductase from Chlorella vulgaris were performed within the pH range 6.0-9.0. Mo(V) was measured by room temperature EPR spectroscopy while the reduction state of FAD was monitored by CD spectroscopy.
Publikováno v:
Plant Physiology. 90:70-74
Initial rate studies of spinach (Spinacia oleracea L.) nitrate reductase showed that NADH:nitrate reductase activity was ionic strength dependent with elevated ionic concentration resulting in inhibition. In contrast, NADH:ferricyanide reductase was
Publikováno v:
Biochemistry. 27:6142-6149
Oxidation-reduction midpoint potentials for flavin, heme, and molybdenum-pterin prosthetic groups of assimilatory nitrate reductase (NR) from Chlorella vulgaris were measured at room temperature by using CD and EPR potentiometry. The CD changes accom