scholarly journals Purification and characterization of the herpes simplex virus type 1 ribonucleotide reductase small subunit following expression in Escherichia coli

1991 ◽  
Vol 72 (6) ◽  
pp. 1383-1392 ◽  
Author(s):  
H. Lankinen ◽  
J. McLauchlan ◽  
M. Weir ◽  
J. Furlong ◽  
J. Conner ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Ribonucleotide Reductase ◽  
Small Subunit ◽  
Purification And Characterization ◽  
Expression In Escherichia Coli ◽  
Simplex Virus

The large subunit of herpes simplex virus type 1 ribonucleotide reductase: Expression in Escherichia coli and purification

Virology ◽  
1991 ◽  
Vol 182 (2) ◽  
pp. 846-851 ◽  
Author(s):  
Judy Furlong ◽  
Joe Conner ◽  
John McLauchlan ◽  
Hilkka Lankinen ◽  
Cathy Galt ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Ribonucleotide Reductase ◽  
Herpes Simplex Virus Type ◽  
Large Subunit ◽  
Expression In Escherichia Coli ◽  
Simplex Virus

scholarly journals Escherichia coli and herpes-simplex-virus ribonucleotide reductase R2 subunit. Compared reactivities of the redox centres

1993 ◽  
Vol 290 (3) ◽  
pp. 807-810 ◽  
Author(s):  
M Atta ◽  
N Lamarche ◽  
J P Battioni ◽  
B Massie ◽  
Y Langelier ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Ribonucleotide Reductase ◽  
Active Sites ◽  
Hydrophobic Interactions ◽  
Chemical Reactivity ◽  
Small Subunit ◽  
Tyrosyl Radical ◽  
Simplex Virus

Protein R2, the small subunit of ribonucleotide reductase, contains a diferric centre and a tyrosyl radical absolutely required for enzyme activity. The reduction of the tyrosyl radical and the mobilization of the iron centre result in the inhibition of the enzyme and thus of DNA synthesis. The chemical reactivity of the iron-radical centre of Escherichia coli and herpes simplex virus has been studied by u.v.-visible and e.p.r. spectroscopies. The tyrosyl radical is efficiently scavenged by hydroxamic acids and phenols during reactions controlled by steric hindrance and hydrophobic interactions. The reaction with o-disubstituted phenols yields the corresponding diphenoquinones. The reactivity of the bacterial radical greatly contrasts with that of the viral radical, and the iron centre in herpes-simplex-virus R2 is much more labile than that in E. coli R2, as shown from the facile mobilization of iron by chelators such as catechol. These results suggest that the active sites of the two enzymes are significantly different and might be useful for designing new antiviral agents.

Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunit

Biochemistry ◽  
1991 ◽  
Vol 30 (7) ◽  
pp. 1939-1947 ◽  
Author(s):  
Graham J. Mann ◽  
Astrid Graeslund ◽  
El Ichiro Ochiai ◽  
Rolf Ingemarson ◽  
Lars Thelander
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Ribonucleotide Reductase ◽  
Purification And Characterization ◽  
Recombinant Mouse ◽  
Ribonucleotide Reductase R2 ◽  
Simplex Virus ◽  
R2 Subunit
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