The Crystal Structure of an Azide Complex of the Diferrous R2 Subunit of Ribonucleotide Reductase Displays a Novel Carboxylate Shift with Important Mechanistic Implications for Diiron-Catalyzed Oxygen Activation

1999 ◽  
Vol 121 (11) ◽  
pp. 2346-2352 ◽  
Author(s):  
Martin E. Andersson ◽  
Martin Högbom ◽  
Agnes Rinaldo-Matthis ◽  
K. Kristoffer Andersson ◽  
Britt-Marie Sjöberg ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribonucleotide Reductase ◽  
Oxygen Activation ◽  
R2 Subunit ◽  
Carboxylate Shift

Crystal Structure of the Ribonucleotide Reductase R2 Mutant that Accumulates a μ-1,2-Peroxodiiron(III) Intermediate during Oxygen Activation

2000 ◽  
Vol 122 (14) ◽  
pp. 3255-3261 ◽  
Author(s):  
Walter C. Voegtli ◽  
Nelly Khidekel ◽  
Jeffrey Baldwin ◽  
Brenda A. Ley ◽  
J. Martin Bollinger, ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribonucleotide Reductase ◽  
Oxygen Activation ◽  
Ribonucleotide Reductase R2

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

scholarly journals Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site

Structure ◽  
1996 ◽  
Vol 4 (9) ◽  
pp. 1053-1064 ◽  
Author(s):  
Derek T Logan ◽  
Xiao-Dong Su ◽  
Anders Åberg ◽  
Karin Regnström ◽  
Janos Hajdu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribonucleotide Reductase ◽  
Oxygen Activation ◽  
Structural Basis ◽  
Iron Site ◽  
Dinuclear Iron

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.

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