Tuning Copper−Dioxygen Reactivity and Exogenous Substrate Oxidations via Alterations in Ligand Electronics

2003 ◽  
Vol 125 (3) ◽  
pp. 634-635 ◽  
Author(s):  
Christiana Xin Zhang ◽  
Hong-Chang Liang ◽  
Eun-il Kim ◽  
Jason Shearer ◽  
Matthew E. Helton ◽  
...  
Keyword(s):  
Exogenous Substrate ◽  
Dioxygen Reactivity ◽  
Copper Dioxygen

scholarly journals Observation of a CuII2(μ-1,2-peroxo)/CuIII2(μ-oxo)2Equilibrium and its Implications for Copper-Dioxygen Reactivity

2014 ◽  
Vol 53 (19) ◽  
pp. 4935-4939 ◽  
Author(s):  
Matthew T. Kieber-Emmons ◽  
Jake W. Ginsbach ◽  
Patrick K. Wick ◽  
Heather R. Lucas ◽  
Matthew E. Helton ◽  
...  
Keyword(s):  
Dioxygen Reactivity ◽  
Copper Dioxygen

Observation of a CuII2(μ-1,2-peroxo)/CuIII2(μ-oxo)2Equilibrium and its Implications for Copper-Dioxygen Reactivity

2014 ◽  
Vol 126 (19) ◽  
pp. 5035-5039 ◽  
Author(s):  
Matthew T. Kieber-Emmons ◽  
Jake W. Ginsbach ◽  
Patrick K. Wick ◽  
Heather R. Lucas ◽  
Matthew E. Helton ◽  
...  
Keyword(s):  
Dioxygen Reactivity ◽  
Copper Dioxygen

scholarly journals Evidence for Copper-dioxygen Reactivity during α-Synuclein Fibril Formation

2010 ◽  
Vol 132 (19) ◽  
pp. 6636-6637 ◽  
Author(s):  
Heather R. Lucas ◽  
Serena DeBeer ◽  
Myoung-Soon Hong ◽  
Jennifer C. Lee
Keyword(s):  
Fibril Formation ◽  
Dioxygen Reactivity ◽  
Copper Dioxygen

Ligand Macrocycle Structural Effects on Copper−Dioxygen Reactivity

2000 ◽  
Vol 39 (18) ◽  
pp. 4059-4072 ◽  
Author(s):  
Bernice M. T. Lam ◽  
Jason A. Halfen ◽  
Victor G. Young, ◽  
John R. Hagadorn ◽  
Patrick L. Holland ◽  
...  
Keyword(s):  
Structural Effects ◽  
Dioxygen Reactivity ◽  
Copper Dioxygen

Modulation of the Copper-Dioxygen Reactivity by Stereochemical Effect of Tetradentate Tripodal Ligands

2002 ◽  
Vol 31 (3) ◽  
pp. 416-417 ◽  
Author(s):  
Hideki Hayashi ◽  
Kounosuke Uozumi ◽  
Shuhei Fujinami ◽  
Shigenori Nagatomo ◽  
Kazushi Shiren ◽  
...  
Keyword(s):  
Tripodal Ligands ◽  
Dioxygen Reactivity ◽  
Copper Dioxygen

Modeling Copper-Dioxygen Reactivity in Proteins: Aliphatic C-H Bond Activation by a New Dicopper(II)-Peroxo Complex

1994 ◽  
Vol 116 (21) ◽  
pp. 9785-9786 ◽  
Author(s):  
Samiran Mahapatra ◽  
Jason A. Halfen ◽  
Elizabeth C. Wilkinson ◽  
Lawrence Que ◽  
William B. Tolman
Keyword(s):  
Bond Activation ◽  
Peroxo Complex ◽  
Dioxygen Reactivity ◽  
Copper Dioxygen

Kinetin-Mediated Stimulation of Accumulation of Buckwheat Flavonoids in the Dark

1983 ◽  
Vol 38 (9-10) ◽  
pp. 711-718 ◽  
Author(s):  
U. Margna ◽  
T. Vainjärv
Keyword(s):  
Anthocyanin Biosynthesis ◽  
Flavonoid Biosynthesis ◽  
Accumulation Rates ◽  
Sharp Rise ◽  
Short Treatment ◽  
Exogenous Substrate ◽  
Percent Increase ◽  
High Level ◽  
Fold Stimulation ◽  
Stimulation Of

A short treatment of excised buckwheat cotyledons with a solution of kinetin lead to an up to 9-fold stimulation of anthocyanin biosynthesis, to an about 50 percent increase in the accumula­tion of rutin, and to an about 30 percent increase, on the average, in the accumulation of C-glycosylflavones in the treated material during its posttreatment incubation in the dark. When the treated cotyledons were incubated in a solution of ʟ--phenylalanine anthocyanin accumulation in the dark practically attained the same high level as it was observed in the illuminated cotyledons fed with exogenous ʟ--phenylalanine. In experiments with l4C-labelled L-phenylalanine kinetin induced a sharp rise in the labelling (resp. in the utilization of exogenous substrate for biosynthesis) of anthocyanins and rutin in the dark and a slight increase in the radioactivity of C-glycosylflavones. Similar labelling changes occurred in the illuminated cotyledons. However, both kinetin and light still more effectively promoted biosynthetic use of the endogenous sub­strate. As a result the relative portion of flavonoids formed from exogenous L-phenylalanine under these conditions showed a decrease as compared with the ratio of precursor use in the un­treated cotyledons. The results show that low accumulation rates of anthocyanins and other flavo­noids in the dark are conditioned by the limited access of substrate (ʟ--phenylalanine) molecules to the flavonoid enzymes lending further support to the idea that flavonoid biosynthesis is normally controlled at the substrate rather than at the enzymic level.

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