Kinetic studies on the reduction of the R2 subunit of mouse ribonucleotide reductase with hydroxyurea, hydrazine, phenylhydrazine and hydroxylamine

1997 ◽  
Vol 2 (3) ◽  
pp. 287-294 ◽  
Author(s):  
Joo-Yeon Han ◽  
Astrid Gräslund ◽  
Lars Thelander ◽  
A. G. Sykes
Keyword(s):  
Ribonucleotide Reductase ◽  
Kinetic Studies ◽  
R2 Subunit

scholarly journals Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity

1996 ◽  
Vol 320 (1) ◽  
pp. 129-135 ◽  
Author(s):  
Nathalie LAMARCHE ◽  
Gilles MATTON ◽  
Bernard MASSIE ◽  
Marc FONTECAVE ◽  
Mohamed ATTA ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Ribonucleotide Reductase ◽  
Binding Capacity ◽  
Eukaryotic Expression ◽  
Eukaryotic Cells ◽  
Expression Systems ◽  
Simplex Virus ◽  
R2 Subunit ◽  
Eukaryotic Expression Systems

The R2 subunit of ribonucleotide reductase from herpes simplex virus type 2 was overproduced with prokaryotic and eukaryotic expression systems. The recombinant R2 purified by a two-step procedure exhibited a 3-fold higher activity when produced in eukaryotic cells. Precise quantification of the R2 concentration at each step of the purification indicated that the activity was not altered during the purification procedure. Moreover, we have observed that the level of R2 expression, in eukaryotic cells as well as in prokaryotic cells, did not influence R2 activity. Extensive characterization of the recombinant R2 purified from eukaryotic and prokaryotic expression systems has shown that both types of pure R2 preparations were similar in their 76 kDa dimer contents (more than 95%) and in their ability to bind the R1 subunit. However, we have found that the higher activity of R2 produced in eukaryotic cells is more probably related to a higher capability of binding the iron cofactor as well as a 3-fold greater ability to generate the tyrosyl free radical.

Magnetic studies of reduced iron clusters in the mouse R2 subunit of ribonucleotide reductase

1995 ◽  
Vol 59 (2-3) ◽  
pp. 372
Author(s):  
K.K. Andersson ◽  
M. Atta ◽  
N. Debaecker ◽  
J.-M. Latour ◽  
L. Thelander ◽  
...  
Keyword(s):  
Ribonucleotide Reductase ◽  
Magnetic Studies ◽  
Iron Clusters ◽  
R2 Subunit

Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis

2003 ◽  
Vol 96 (1) ◽  
pp. 235
Author(s):  
Pal Stenmark ◽  
Martin Högbom ◽  
Pär Nordlund ◽  
Grant McClarty
Keyword(s):  
Crystal Structure ◽  
Chlamydia Trachomatis ◽  
Ribonucleotide Reductase ◽  
R2 Subunit

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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