A stable FeIII-FeIV replacement of tyrosyl radical in a class I ribonucleotide reductase

Biochemical and Biophysical Research Communications

Volumn 330, Issue 4, 2005, Pages 1213-1216

  Voevodskaya, N ^a   Lendzian, F ^b   Graslund A ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Chlamydia trachomatis; EPR spectroscopy; FeIII FeIV site; Ribonucleotide reductase; Species X; Tyrosyl radical

Indexed keywords

IRON; RADICAL; RIBONUCLEOTIDE REDUCTASE; TYROSINE; PHENYLALANINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CHLAMYDIA TRACHOMATIS; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; OXIDATION; PRIORITY JOURNAL; CHEMISTRY; ENZYMOLOGY; OXIDATION REDUCTION REACTION; PROTEIN BINDING;

CHLAMYDIA TRACHOMATIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; IRON; OXIDATION-REDUCTION; PHENYLALANINE; PROTEIN BINDING; RIBONUCLEOTIDE REDUCTASES; TYROSINE;

EID: 17044390320     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.03.104     Document Type: Article

References (20)

1. J. Schather, in: R.S. Stephens (Ed.), Chlamydia: Intracellular Biology, Pathogenesis and Immunity, American Society for Microbiology, Washington, DC, 1999, pp. 69-100
2. P. Reichard From RNA to DNA, why so many ribonucleotide reductases? Science 260 1993 1773 1777
3. B.-M. Sjöberg Ribonucleotide reductases-a group of enzymes with different metallosites and a similar reaction mechanism Struct. Bonding 88 1997 139 173
4. J. Stubbe, D.G. Nocera, C.S. Yee, and C.Y. Chang Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer? Chem. Rev. 103 2003 2167 2201
5. H. Eklund, U. Uhlin, M. Färnegårdh, D.T. Logan, and P. Nordlund Structure and function of the radical enzyme ribonucleotide reductase Progr. Biophys. Mol. Biol. 77 2001 177 268
6. C. Roshick, E.R. Iliffe-Lee, and G.J. McClarty Cloning and characterization of ribonucleotide reductase from Chlamydia trachomatis J. Biol. Chem. 275 2000 38111 38119
7. P. Stenmark, M. Högbom, C. Roshick, G. McClarty, and P. Nordlund Crystals of the ribonucleotide reductase R2 protein from Chlamydia trachomatis obtained by heavy-atom co-crystallization Acta Cryst. D Biol. Crystallogr. 60 2004 376 378
8. M. Högbom, P. Stenmark, N. Voevodskaya, G. McClarty, A. Gräslund, and P. Nordlund The radical site in Chlamydial ribonucleotide reductase defines a new R2 subclass Science 305 2004 245 248
9. J.M. Bollinger Jr., D.E. Edmondson, B.H. Huynh, J. Filley, J.R. Norton, and J. Stubbe Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase Science 253 1991 292 298
10. J.M. Bollinger Jr., J. Stubbe, B.H. Huynh, and D.E. Edmondson Novel diferric radical intermediate responsible for tyrosyl radical formation in assembly of the cofactor of ribonucleotide reductase J. Am. Chem. Soc. 113 1991 6289 6291
11. N. Ravi, J.M. Bollinger Jr., B.H. Huynh, D.E. Edmondson, and J. Stubbe Mechanism of assembly of the tyrosyl radical-diiron(III) cofactor of E. coli ribonucleotide reductase: 1. Mössbauer characterization of the diferric radical precursor J. Am. Chem. Soc. 116 1994 8007 8014
12. B.E. Sturgeon, D. Burdi, S. Chen, B.H. Huynh, D.E. Edmondson, J. Stubbe, and B.M. Hoffman Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase J. Am. Chem. Soc. 118 1996 7551 7557
13. S. Pötsch, F. Lendzian, R. Ingemarson, A. Hörnberg, L. Thelander, W. Lubitz, G. Lassmann, and A. Gräslund The iron-oxygen reconstitution reaction in protein R2-Y177 mutants of mouse ribonucleotide reductase. EPR and ENDOR studies on a new transient tryptophan radical J. Biol. Chem. 274 1999 17696 17704
14. J. Baldwin, C. Krebs, B.A. Ley, D.E. Edmondson, B.H. Huynh, and J.M. Bollinger Jr. Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical J. Am. Chem. Soc. 122 2000 12195 12206
15. D. Yun, C. Krebs, G.P. Gupta, D.F. Iwig, B.H. Huynh, and J.M. Bollinger Jr. Facile electron transfer during formation of cluster X and kinetic competence of X for tyrosyl radical production in protein R2 of ribonucleotide reductase from mouse Biochemistry 41 2002 981 990
16. R. Davis, M. Thelander, G.J. Mann, G. Behravan, F. Soucy, P. Beaulieu, P. Lavallee, A. Gräslund, and L. Thelander Purification, characterization, and localization of subunit interaction area of recombinant mouse ribonucleotide reductase R1 subunit J. Biol. Chem. 269 1994 23171 23176
17. 57Fe Mössbauer spectroscopy: monitoring changes of an iron-containing active site during a biochemical reaction Inorg. Chem. 44 2005 742 757
18. M. Kolberg, D.T. Logan, G. Bleifuss, S. Pötsch, B.-M. Sjöberg, A. Gräslund, W. Lubitz, G. Lassmann, and F. Lendzian A new tyrosyl radical on Phe208 as ligand to the diiron center in Escherichia coli ribonucleotide reductase, mutant R2-Y122H J. Biol. Chem. 280 2005 11233 11246
19. U. Uhlin, and H. Eklund The ten-stranded β/α barrel in ribonucleotide reductase protein R1 J. Mol. Biol. 262 1996 358 369
20. P. Nordlund, and H. Eklund Structure and function of the Escherichia coli ribonucleotide reductase protein R2 J. Mol. Biol. 232 1993 123 164