The alkoxy radical, RCH2Ȯ, as a free radical product in x-irradiated single crystals of nucleosides and nucleotides

1977 ◽  
Vol 67 (3) ◽  
pp. 1211 ◽  
Author(s):  
William A. Bernhard ◽  
David M. Close ◽  
Jürgen Hüttermann ◽  
Herbert Zehner
1978 ◽  
Vol 6 (5) ◽  
pp. 962-964 ◽  
Author(s):  
A. INGALL ◽  
K. A. K. LOTT ◽  
T. F. SLATER ◽  
S. FINCH ◽  
A. STIER

2004 ◽  
Vol 71 ◽  
pp. 39-49 ◽  
Author(s):  
Dennis J. Stuehr ◽  
Chin-Chuan Wei ◽  
Jerome Santolini ◽  
Zhi- Qiang Wang ◽  
Mika Aoyagi ◽  
...  

NOSs (nitric oxide synthases) are flavohaem enzymes that function broadly in human health and disease. We are combining mutagenesis, crystallographic and rapid kinetic methods to understand their mechanism and regulation. The NOSs create a transient tetrahydrobiopterin radical within the enzyme to generate their free radical product (NO). Recent work is revealing how critically important this process is at all levels of catalysis. This article will synthesize four seemingly disparate but related aspects of NOS tetrahydrobiopterin radical formation: (i) how it enables productive O2 activation by providing an electron to the enzyme haem, (ii) what structural features help to regulate this electron transfer, (iii) how it enables NOS to synthesize NO from its diamagnetic substrate and (iv) how it allows NOS to release NO after each catalytic cycle instead of other nitorgen oxide-containing products.


1974 ◽  
Vol 3 (2) ◽  
pp. 125-128 ◽  
Author(s):  
Mitsuo Namiki ◽  
Midori Yano ◽  
Tateki Hayashi

1972 ◽  
Vol 129 (2) ◽  
pp. 273-283 ◽  
Author(s):  
S. N. Young ◽  
G. Curzon

1. The curved plots of 1/v against 1/[S] obtained when caeruloplasmin oxidizes NN-dimethyl-p-phenylenediamine were investigated. The first free-radical oxidation product of caeruloplasmin oxidation of NN-dimethyl-p-phenylenediamine is required for curvature, as straight-line plots were obtained when activities were measured either before appreciable free-radical product had appeared or in the presence of ascorbate, which reduced it back to NN-dimethyl-p-phenylenediamine. 2. In the presence of ascorbate linear reciprocal-plots were obtained with all of the 37 substrates tested. Vmax. values varied over only an eightfold range and those for the 20 p-amino compounds over only a twofold range. Km values, however, varied over a 104-fold range. The small range of Vmax. values indicates that the rate-limiting step in caeruloplasmin action is relatively independent of the nature of the substrate. Km values suggest that substrates bind primarily by ring electrons, although certain side-chain groups increased the Km in a manner unrelated to likely changes of ring-electron densities. A mechanism involving repulsion between negative charges on the substrate and the enzyme was supported by the variation of the Km of 5-hydroxyindol-3-ylacetic acid with pH.


1979 ◽  
Vol 77 (1) ◽  
pp. 62 ◽  
Author(s):  
I. Egtvedt ◽  
E. Sagstuen ◽  
T. Henriksen
Keyword(s):  

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