A Photoinduced Chemiluminescence of Riboflavin in Water Containing Hydrogen Peroxide II. Photochemical Aromatic Hydroxylation*

Biochemistry ◽  
1965 ◽  
Vol 4 (5) ◽  
pp. 814-822 ◽  
Author(s):  
J. Richard Williams ◽  
Richard H. Steele
1991 ◽  
Vol 69 (2) ◽  
pp. 215-222 ◽  
Author(s):  
Akikazu Itoh ◽  
Yasushi Kuroda ◽  
Tomoyuki Kitano ◽  
Guo Zhi-Hu ◽  
Atsutaka Kunai ◽  
...  

2007 ◽  
Vol 2007 (27) ◽  
pp. 4253-4253
Author(s):  
Poulami Pattanayak ◽  
Jahar Lal Pratihar ◽  
Debprasad Patra ◽  
Andrew Burrows ◽  
Mary Mohan ◽  
...  

2015 ◽  
Vol 44 (39) ◽  
pp. 17261-17267 ◽  
Author(s):  
Ambica Kejriwal ◽  
Pinaki Bandyopadhyay ◽  
Achintesh N. Biswas

Aromatic hydroxylation catalyzed by a nonheme diiron(iii) complex with hydrogen peroxide at room temperature is described.


2007 ◽  
Vol 2007 (27) ◽  
pp. 4263-4271 ◽  
Author(s):  
Poulami Pattanayak ◽  
Jahar Lal Pratihar ◽  
Debprasad Patra ◽  
Andrew Burrows ◽  
Mary Mohan ◽  
...  

1978 ◽  
Vol 170 (3) ◽  
pp. 693-698 ◽  
Author(s):  
J Chrastil ◽  
J T Wilson

Hydroxylation systems containing cytochromes, proteins and ascorbic acid were studied at physiological pH (7.4) under O2 or N2 with added H2O2. Proteins inhibited aromatic hydroxylation of p-nitrophenol or oxidative demethylation of ethylmorphine in ascorbic acid-containing systems incubated under O2, but strongly activated the systems containing H2O2. Cytochrome c and partially purified cytochrome P-450 from rat liver microsomal preparations activated the system in either O2 or H2O2. The systems needed ascorbic acid (or other enol structures) for activation. Cytochrome iron participated probably in the activation of O2, whereas cytochrome protein participated in a free radical activation of H2O2 (or of O2).


1971 ◽  
Vol 36 (21) ◽  
pp. 3184-3187 ◽  
Author(s):  
Michael E. Kurz ◽  
Glen J. Johnson

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