Ribonucleotide reductase - Structural studies of a radical enzyme

Biological Chemistry

Volumn 378, Issue 8, 1997, Pages 821-825

  Eklund, Hans ^a   Eriksson, Mathias ^a   Uhlin, Ulla ^a   Nordlund, Pär ^b   Logan, Derek ^b  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Allosteric regulation; Di iron protein; Radical transfer; Redox active cysteines; Substrate binding; Tyrosyl radical

Indexed keywords

FREE RADICAL; NUCLEOTIDE; RIBONUCLEOTIDE REDUCTASE; TYROSINE;

ALLOSTERISM; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; REVIEW;

ESCHERICHIA COLI; MOLECULAR CONFORMATION; RIBONUCLEOTIDE REDUCTASES;

ESCHERICHIA COLI;

EID: 0030762177     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (19)

1. Climent, I., Sjöberg, B.-M., and Huang, C.Y. (1992). Site directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Biochemistry 31, 4801-4807.
2. Ekberg, M., Sahlin, M., Eriksson, M., and Sjöberg, B.-M. (1996). Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase. J. Biol. Chem. 271, 20655-20659.
3. Eriksson, M., Uhlin, U., Ramaswamy, S., Ekberg, M., Regnström, K., Sjöberg, B.-M., and Eklund, H. (1997). Binding of substrate and allosteric effectors to ribonucleotide reductase protein R1, substrate binding requires reduced active site cysteines. Structure, in press.
4. Kauppi, B., Nielsen, B.A., Ramaswamy, S., Kjøller Larsen, I., Thelander, M., Thelander, L., and Eklund, H. (1996). The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. J. Mol. Biol. 262, 706-720.
5. Knappe, J., Elberg, S., Frey, M., and Wagner, A.F.V. (1993). Pyruvate formate-lyase mechanism involving the protein-based glycyl radical. Biochem. Soc. Trans. 21, 731-734.
6. Larsson, Å., and Sjöberg, B.-M. (1986). Identification of the stable free radical tyrosine residue in ribonucleotide reductase. EMBO J. 5, 2037-2040.
7. Lipscomb, J.D. (1994). Biochemistry of the soluble methane monooxygenase. Annu. Rev. Microbiol. 48, 371-399.
8. Logan, D.T., Su, X.D., Åberg, A., Regnström, K., Hajdu, J., Eklund, H., and Nordlund, P. (1996). Crystal structure of reduced protein R2 of ribonucleotide reductase: The structural basis for oxygen activation at a dinuclear iron site. Structure 4, 1053-1064.
9. Mao, S.S., Holler, T.P., Yu, G.X., Bollinger, J.-M., Booker, S., Johnston, M.I., and Stubbe, J. (1992). A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing. Biochemistry 31, 9733-9743.
10. Nordlund, P., and Eklund, H. (1993). Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. Mol. Biol. 232, 123-164.
11. Nordlund, P., Sjöberg, B.-M., and Eklund, H. (1990). Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593-598.
12. Que, L.J., and Dong, Y. (1996). Modeling the oxygen activation chemistry of methane monooxygenase and ribonucleotide reductase. Acc. Chem. Res. 29, 190-196.
13. Reichard, P. (1993). From RNA to DNA, why so many ribonucleotide reductases? Science 260, 1773-1777.
14. Reichard, P., and Ehrenberg, A. (1983). Ribonucleotide reductase - a radical enzyme. Science 221, 514-519.
15. Rova, U., Goodtzova, K., Ingemarson, R., Behravan, G., Gräslund, A., and Thelander, L. (1995). Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase. Biochemistry 34, 4267-4275.
16. Sjöberg, B.-M. (1994). The ribonucleotide reductase jigsaw puzzle: A large piece falls into place. Structure 2, 793-796.
17. Stryer, L. (1995). Biochemistry, 4th ed., (New York: Freeman and Company).
18. Thelander and Reichard, P. (1979). Reduction of ribonucleotides. Ann. Rev. Biochem. 48, 133-158.
19. Uhlin, U., and Eklund, H. (1994). Structure of ribonucleotide reductase protein R1. Nature 370, 533-539.