نتایج جستجو برای: zinc borohydride
تعداد نتایج: 75081 فیلتر نتایج به سال:
Correction for 'In situ study of the catalytic mechanism for the oxygen reduction reaction on a polypyrrole modified carbon supported cobalt hydroxide cathode in direct borohydride fuel cells' by Haiying Qin et al., Phys. Chem. Chem. Phys., 2013, 15, 9070-9074.
Studies directed at the amine exchange reaction of vinamidinium salts followed by sodium borohydride reduction to secondary and tertiary allylic amines are described. The tertiary allylic amines were alkylated and subjected to base mediated rearrangement to yield a variety of highly functionalized tertiary homoallylic amines.
Atomically ordered nickel carbide, Ni3C, was synthesized by reduction of nickel cyclopentadienyl (NiCp2) with sodium naphthalide to form Ni clusters coordinated by Cp (Ni-Cp clusters). Ni-Cp clusters were thermally decomposed to Ni3C nanoparticles smaller than 10 nm. The Ni3C nanoparticles showed better performance than Ni nanoparticles and Au nanoparticles in the electrooxidation of sodium bor...
Sodium-2-oxo-propanesulfonate (acetone sulfonate) was found to be a competitive inhibitor of acetoacetate carboxy lyase (acetoacetic decarboxylase, EC 4.1.1.4) the KI of which was numerically equal to the K, for acetoacetate at all temperatures investigated. K,,, like Kr in this case is therefore concluded to represent a dissociation constant. AH for the dissociation of either acetoacetate or a...
The verdin-type Chromophore of denatured C-phycocyanin (1) from Spirulina platensis is reduced to the corresponding rubin (2 a) by sodium borohydride. The structure assigned is in agreement with the uv-vis spectroscopic properties of the product and was deduced from model studies with free bile pigments. Analogous model studies using sodium dithionite demonstrated a two-fold reactivity for this...
The pyruvate-aspartic semialdehyde condensing enzyme, which occurs at the branch point in the aspartic acid family of amino acids leading to diaminopimelic acid and lysine biosynthesis, has been purified 5000-fold from crude extracts of Escherichia coli W. The protein has been shown to be homogeneous by polyacrylamide gel electrophoresis and bears a net negative charge in the pH range 6.0 to 9....
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