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Publications by J. Martin Bollinger, Jr.

2007

Fujimori, D. G., E. W. Barr, M. L. Matthews, G. M. Koch, J. R. Yonce, C. T. Walsh, J. M. Bollinger, Jr., C. Krebs, and P. J. Riggs-Gelasco. Spectroscopic evidence for a high-spin Br-Fe(IV)-oxo intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces. J. Am. Chem. Soc. 129:13408-13409.

Neidig, M. L., C. D. Brown, K. M. Light, D. G. Fujimori, E. M. Nolan, J. C. Price, E. W. Barr, J. M. Bollinger, Jr., C. Krebs, C. T. Walsh, and E. I. Solomon. CD and MCD of CytC3 and taurine dioxygenase: Role of the facial triad in α-KG-dependent dioxygenases. J. Am. Chem. Soc. 129:14224-14231.

Eser, B., E. W. Barr, P. A. Frantom, L. Saleh, J. M. Bollinger, Jr., C. Krebs, and P. F. Fitzpatrick. Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. J. Am. Chem. Soc. 129:11334-11335.

Jiang, W., L. M. Hoffart, C. Krebs, and J. M. Bollinger, Jr. A Mn(IV)/Fe(IV) intermediate in assembly of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase. Biochemistry 46:8709-8716.

Krebs, C., M. L. Matthews, W. Jiang, and J. M. Bollinger, Jr. AurF from Streptomyces thioluteus and a possible new family of manganese/iron oxygenases. Biochemistry 46:10413-10418.

Jiang, W., J. M. Bollinger, Jr., and C. Krebs. The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state. J. Am. Chem. Soc. 129:7504-7505.

Sinnecker, S., N. Svensen, E. W. Barr, S. Ye, J. M. Bollinger, Jr., F. Neese, and C. Krebs.
Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-Oxo intermediates in taurine:α-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant. J. Am. Chem. Soc. 129:6168-6179.

Jiang, W., D. Yun, L. Saleh, E. W. Barr, G. Xing, L. M. Hoffart, M. A. Maslak, C. Krebs, and J. M. Bollinger, Jr. A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase. Science 316:1188-1191.

Galonic, D. P., E. W. Barr, C. T. Walsh, J. M. Bollinger, Jr., and C. Krebs. Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3. Nat. Chem. Biol. 3:113-116.

Bollinger, J. M., Jr. and C. Krebs. Enzymatic C-H activation by metal-superoxo intermediates. Curr. Opin. Chem. Biol. 11:151-158.

Krebs, C., D. G. Fujimori, C. T. Walsh, and J. M. Bollinger, Jr. Non-heme Fe(IV)-oxo intermediates. Acc. Chem. Res. 40:484-492.

Yun, D., L. Saleh, R. Garcia-Serres, B. M. Chicalese, Y. H. An, B. H. Huynh, and J. M. Bollinger, Jr. Addition of oxygen to the Diiron(II/II) cluster is the slowest step in formation of the tyrosyl radical in the W 103Y variant of ribonucleotide reductase protein R2 from mouse. Biochemistry 46:13067-13073.

Mitic, N., M. D. Clay, L. Saleh, J. M. Bollinger, Jr., and E. I. Solomon. Spectroscopic and electronic-structure studies of intermediate X in ribonucleotide reductase R2 and two variants: A description of the FeIV-Oxo bond in the FeIII-O-FeIV dimer. J. Am. Chem. Soc. 129:9049-9065.

Yun, D., R. Garcia-Serres, B. M. Chicalese, Y. H. An, B. H. Huynh, and J. M. Bollinger, Jr. A μ-1,2-peroxodiiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X, in assembly of the iron-radical cofactor of ribonucleotide reductase from mouse. Biochemistry 46:1925-1932.

2006

Hoffart, L. M., E. W. Barr, R. B. Guyer, J. M. Bollinger, Jr., and C. Krebs. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a Prolyl-4-hydroxylase. Proc. Natl. Acad. Sci. USA 103:14738-14743.

Saleh, L. and J. M. Bollinger, Jr. Cation mediation of radical transfer between Trp48 and Tyr356 during O2 activation by protein R2 of Escherichia coli ribonucleotide reductase: relevance to R1-R2 radical transfer in nucleotide reduction? Biochemistry 45:8823-8830.

Kim, S. H., G. Xing, J. M. Bollinger, Jr., C. Krebs, and B. M. Hoffman. Demonstration by 2H ENDOR spectroscopy that myo-inositol binds via an alkoxide bridge to the mixed-valent diiron center of myo-inositol oxygenase. J. Am. Chem. Soc. 128:10374-10375.

Yeh, E., L. J. Cole, E. W. Barr, J. M. Bollinger, Jr., D. B. Ballou, and C. T. Walsh. Flavin redox chemistry precedes substrate chlorination during reaction of the flavin-dependent halogenase RebH. Biochemistry 45:7904-7912.

Xing, G., Y. Diao, L. M. Hoffart, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr. Novel mechanisms of oxygen activation and C-H cleavage by a dinuclear iron cluster in myo-inositol oxygenase. Proc. Natl. Acad. Sci. USA 103:6130-6135.

Xing, G., L. M. Hoffart, Y. Diao, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr. Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol-cleavage reaction catalyzed by myo-inositol oxygenase. Biochemistry 45:5402-5412.

Xing, G., L. M. Hoffart, Y. Diao, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr. Spectroscopic evidence for a coupled dinuclear iron cluster that coordinates the substrate in myo-inositol oxygenase. Biochemistry 45:5393-5401.

Bollinger, J. M., Jr. and C. Krebs. Stalking intermediates in oxygen activation by iron enzymes: Motivation and method. J. Inorg. Biochem. 100:586-605

2005

Bollinger, J. M. Jr., J. C. Price, L. M. Hoffart, E. W. Barr, and C. Krebs. Mechanism of taurine: a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Eur. J. Inorg. Chem. 21:4245-4254.

Sommerhalter, M., L. Saleh, J.M. Bollinger, Jr., and A. C. Rosenzweig. Structure of Escherichia coli ribonucleotide reductase R2 in space group P6(1)22. Acta Cryst. D61:1649-1654.

Price, J. C., E. W. Barr, L. M. Hoffart, C. Krebs, and J.M. Bollinger, Jr. Kinetic dissection of the catalytic mechanism of taurine: a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 44:8138-8147.

Krebs, C., J. C. Price, J. Baldwin, L. Saleh, M. T. Green, and J.M. Bollinger, Jr. Rapid freeze-quench57Fe-Mössbauer spectroscopy: Monitoring changes of an iron-containing active site during a biochemical reaction. Inorg. Chem. 44:742-757.

Shen, G., R. Balasubramanian, T. Wang, B. Tirupati, J.M. Bollinger, Jr., J. H. Golbeck, and D. A. Bryant. Functional genomics of genes for biogenesis of Fe-S proteins in cyanobacteria. In: Photosynthesis: Fundamental Aspects to Global Perspectives, Proceedings of the XIIIth International Congress on Photosynthesis, Montreal. (A. van der Est and D. Bruce, eds.), pp. 882-884, Allen Press, Lawrence, KA.

2004

Saleh, L., B.A. Kelch, B.A. Pathickal, J. Baldwin, B.A. Ley, and J.M. Bollinger, Jr. Mediation by indole analogues of electron transfer during oxygen activation in variants of Escherichia coli ribonucleotide reductase R2 lacking the electron-shuttling tryptophan 48. Biochemistry 43:5943-5952.

Saleh, L., C. Krebs, B.A. Ley, S. Naik, B.H. Huynh, and J.M. Bollinger, Jr. Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase. Biochemistry 43:5953-5964.

Wei, P.-p., A.J. Skulan, N. Mitic, Y.-S. Yang, L. Saleh, J.M. Bollinger, Jr., and E.I. Solomon. Electronic and spectroscopic studies of the non-heme reduced binuclear iron sites of two ribonucleotide reductase variants: comparison to reduced methane monooxygenase and contributions to O₂ reactivity. J. Am. Chem. Soc. 126:3777-3788.

Behshad, E., S.E. Parkin, and J.M. Bollinger, Jr. Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: kinetic analysis of cleavage of the persulfide intermediate by chemical reductants. Biochemistry 43:12220-12226.

Tirupati, B., J.L. Vey, C.L. Drennan, and J.M. Bollinger, Jr. Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803. Biochemistry 43:12210-12219.

Lu, S., E. Libby, L. Saleh, G. Xing, J.M. Bollinger, Jr., and P. Moenne-Loccoz. Characterization of NO adducts of the diiron center in protein R2 of Escherichia coli ribonucleotide reductase and site-directed variants; implications for the O₂ activation mechanism. J. Biol. Inorg. Chem. 9:818-827.

Skulan, A.J., T.C. Brunold, J. Baldwin, L. Saleh, J.M. Bollinger, Jr., and E.I. Solomon. Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant: implication for O₂ activation by binuclear non-heme iron enzymes. J. Am. Chem. Soc. 126:8842-8855.

Riggs-Gelasco, P.J., J.C. Price, R.B. Guyer, J.H. Brehm, E.W. Barr, J.M. Bollinger, Jr., and C. Krebs. EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by Taurine:a-ketoglutarate dioxygenase. J. Am. Chem. Soc. 126:8108-8109.

2003

Baldwin, J., C. Krebs, L. Saleh, M. Stelling, B.H. Huynh, J.M. Bollinger, Jr., and P. Riggs-Gelasco. Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli. Biochemistry 42:13269-13279.

Voegtli, W.C., M. Sommerhalter, L. Saleh, J. Baldwin, J.M. Bollinger, Jr., and A.C. Rosenzweig. Variable coordination geometries at the diiron(II) active site of ribonucleotide reductase R2. J. Am. Chem. Soc. 125:15822-15830.

Price, J.C., E.W. Barr, B. Tirupati, J.M. Bollinger, Jr., and C. Krebs. The first direct characterization of a high-valent iron intermediate in the reaction of an a-ketoglutarate-dependent dioxygenase: A high-dpin Fe(IV) complex in taurine/a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42:7497-7508.

Mitic, N., L. Saleh, G. Schenk, J.M. Bollinger, Jr., and E.I. Solomon. Rapid-freeze-quench magnetic circular dichroism of intermediate X in ribonucleotide reductase: new structural insight. J. Am. Chem. Soc. 125:11200-11201.

Price, J.C., E.W. Barr, T.E. Glass, C. Krebs, and J.M. Bollinger, Jr. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine: a-ketoglutarate dioxygenase (TauD). J. Am. Chem. Soc. 125:13008-13009.

2002

Yun, D., 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. 41:981-990.

Krebs, C., J.M. Bollinger, Jr., E.C. Thiel, and B.H. Huynh. Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy. J. Biol. Inorg. Chem. 7:863-869.

2001

Yun, D., 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 protien R2 of ribonucleotide reductase from mouse. Biochemistry. 41:981-990.

Baldwin, J., W.C. Voegtli, N. Khidekel, P. Moenne-Loccoz, C. Krebs, A.S. Pereira, B.A. Ley, B.H. Huynh, T.M. Loehr, P.J. Riggs-Gelasco, A.C. Rosenzweig, and J.M. Bollinger, Jr. Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase. J. Am. Chem. Soc. 123:7017-7030.

2000

Voegtli, W.C., N. Khidekel, J. Baldwin, B.A. Ley, J.M. Bollinger, Jr., and A.C. Rosenzweig. Crystal Structure of the Ribonucleotide Reductase R2 Mutant that Accumulates a m-1,2-peroxodiiron(III) Intermediate During Oxygen Activation. J. Am. Chem. Soc. 122:3255-3261.

Krebs, C., R. Davydov, J. Baldwin, B.M. Hoffman, J.M. Bollinger, Jr., and B.H. Huynh. Mössbauer and EPR Characterization of the S = 9/2 Mixed-valence Fe(II)Fe(III) Cluster in Cryoreduced R2 Subunit of Escherichia coli Ribonucleotide Reductase. J. Am. Chem. Soc. 122:5327-5336.

Yang, Y.-S., J. Baldwin, B.A. Ley, J.M. Bollinger, Jr., and E.I. Solomon. Spectroscopic and Electronic Structure Description of the Reduced Binuclear Non-heme Iron Active Site in Ribonucleotide Reductase from E. coli: Comparison to Reduced D9 Desaturase and Electronic Structure Contributions to Differences in O2 Reactivity. J. Am. Chem. Soc. 122:8495-8510.

Baldwin, J., C. Krebs, B.A. Ley, 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. 122:12195-12206.

Krebs, C., S. Chen, J. Baldwin, B.A. Ley, U. Patel, 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. 2. Evidence for and Consequences of Blocked Electron Transfer in the W48F Variant. J. Am. Chem. Soc. 122:12207-12219.

1998

Bollinger, J.M., Jr., C. Krebs, A. Vicol, S. Chen, B.A. Ley, D.E. Edmondson, and B.H. Huynh. Engineering the Diiron Site of Escherichia coli Ribonucleotide Reductase Protein R2 to Accumulate an Intermediate Similar to Hperoxo, the Putative Peroxodiiron(III) Complex from the Methane Monooxygenase Catalytic Cycle. J. Am. Chem. Soc. 120:1094-1095.

Huynh, B.H., J.M. Bollinger, Jr., and D.E. Edmondson. Reaction Intermediates in Oxygen Activation by Enzymes Containing Carboxylate-bridged Binuclear Iron Clusters. In: Spectroscopic Methods in Bioinorganic Chemistry. (E. I. Solomon and K. O. Hodgson, eds.), pp. 403-422, American Chemical Society, Washington, D.C.

Moënne-Loccoz, P., J. Baldwin, B.A. Ley, T.M. Loehr, and J.M. Bollinger, Jr. O₂ Activation by Non-heme Diiron Proteins: Identification of a Symmetric m-1,2-peroxide in a Mutant of Ribonucleotide Reductase. Biochemistry. 37:14659-14663.

Parkin, S.E., S. Chen, B.A. Ley, L. Mangravite, D.E. Edmondson, B.H. Huynh, and J.M. Bollinger, Jr. Electron Injection Through a Specific Pathway Determines the Outcome of Oxygen Activation at the Diiron Cluster in the F208Y Mutant of Escherichia coli Ribonucleotide Reductase Protein R2. Biochemistry. 37:1124-1130.

1997

J.M. Bollinger, Jr., C. Krebs, A. Vicol, S. Chen, B.A. Ley, D.E. Edmondson, and B.H. Huynh. Engineering the Diiron Site of Escherichia coli Ribonucleotide Reductase Protein R2 to Accumulate an Intermediate Similar to H_peroxo, the Putative Peroxodiiron (III) Complex from the Methane Monooxygenase Catalytic Cycle. J. Am. Chem. Soc. 120:1094-1095.

D.S. Kwon, C.-H. Lin, S. Chen, J.K. Coward, C.T. Walsh, and J.M. Bollinger, Jr. Dissection of Glutathionylspermidine Synthetase/Amidase from Escherichia coli into Autonomously Folding and Functional Synthetase and Amidase Domains. J. Biol. Chem. 272:2429-2436.

Lin, C.-H., D.S. Kwon, J.M. Bollinger, Jr., and C.T. Walsh. Evidence for a Glutathionyl-Enzyme Intermediate in the Amidase Activity of The Bifunctional Glutathionylspermidine Synthetase/Amidase from Escherichia coli. Biochemistry. 36:14930-14938.

Parkin, S.E., S. Chen, B.A. Ley, L. Mangravite, D.E. Edmondson, B.H. Huynh, and J.M. Bollinger, Jr. Electron Injection through a Specific Pathway Determines the Outcome of Oxygen Activation at the Diiron Cluster in the F208Y Mutant of Escherichia coli Ribonucleotide Reductase Protein R2. Biochemistry. 37:1124-1130.

1995

Bollinger, J.M., Jr., D.S. Kwon, G.W. Huisman, R. Kolter, and C.T. Walsh. Glutathionylspermidine Metabolism in E. coli: Purification, Cloning, Overproduction and Characterization of a Bifunctional Glutathionylspermidine Synthetase/Amidase. J. Biol. Chem. 270:l403l-l404l.

Bollinger, J.M., Jr., W.H. Tong, N. Ravi, B.H. Huynh, D.E. Edmondson, and J. Stubbe. Use of Rapid Kinetics Methods to Study the Assembly of the Diferric-Tyrosyl Radical Cofactor of E. coli Ribonucleotide Reductase. Methods Enzymol. 258:278-303.

Hidalgo, E., J.M. Bollinger, Jr., T.M. Bradley, C.T. Walsh, B. Demple. Binuclear FeS Centers in the Escherichia coli SoxR Protein and Role of the Metal Centers in Transcription. J. Biol. Chem. 270:20908-209l4.

Pulver, S.C., W.H. Tong, J.M. Bollinger, Jr., J. Stubbe, and E.I. Solomon. Circular Dichroism and Magnetic Circular Dichroism Studies of the Fully Reduced Binuclear Non-Heme Iron Active Site in the Escherichia coli R2 Subunit of Ribonucleoside Diphosphate Reductase. J. Am. Chem. Soc. ll7:l2664-l2687.


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About Us Faculty Facilities Seminars Publications News and Events Outreach Links	Publications by J. Martin Bollinger, Jr. 2007 Fujimori, D. G., E. W. Barr, M. L. Matthews, G. M. Koch, J. R. Yonce, C. T. Walsh, J. M. Bollinger, Jr., C. Krebs, and P. J. Riggs-Gelasco. Spectroscopic evidence for a high-spin Br-Fe(IV)-oxo intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces. J. Am. Chem. Soc. 129:13408-13409. Neidig, M. L., C. D. Brown, K. M. Light, D. G. Fujimori, E. M. Nolan, J. C. Price, E. W. Barr, J. M. Bollinger, Jr., C. Krebs, C. T. Walsh, and E. I. Solomon. CD and MCD of CytC3 and taurine dioxygenase: Role of the facial triad in α-KG-dependent dioxygenases. J. Am. Chem. Soc. 129:14224-14231. Eser, B., E. W. Barr, P. A. Frantom, L. Saleh, J. M. Bollinger, Jr., C. Krebs, and P. F. Fitzpatrick. Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. J. Am. Chem. Soc. 129:11334-11335. Jiang, W., L. M. Hoffart, C. Krebs, and J. M. Bollinger, Jr. A Mn(IV)/Fe(IV) intermediate in assembly of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase. Biochemistry 46:8709-8716. Krebs, C., M. L. Matthews, W. Jiang, and J. M. Bollinger, Jr. AurF from Streptomyces thioluteus and a possible new family of manganese/iron oxygenases. Biochemistry 46:10413-10418. Jiang, W., J. M. Bollinger, Jr., and C. Krebs. The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state. J. Am. Chem. Soc. 129:7504-7505. Sinnecker, S., N. Svensen, E. W. Barr, S. Ye, J. M. Bollinger, Jr., F. Neese, and C. Krebs. Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-Oxo intermediates in taurine:α-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant. J. Am. Chem. Soc. 129:6168-6179. Jiang, W., D. Yun, L. Saleh, E. W. Barr, G. Xing, L. M. Hoffart, M. A. Maslak, C. Krebs, and J. M. Bollinger, Jr. A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase. Science 316:1188-1191. Galonic, D. P., E. W. Barr, C. T. Walsh, J. M. Bollinger, Jr., and C. Krebs. Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3. Nat. Chem. Biol. 3:113-116. Bollinger, J. M., Jr. and C. Krebs. Enzymatic C-H activation by metal-superoxo intermediates. Curr. Opin. Chem. Biol. 11:151-158. Krebs, C., D. G. Fujimori, C. T. Walsh, and J. M. Bollinger, Jr. Non-heme Fe(IV)-oxo intermediates. Acc. Chem. Res. 40:484-492. Yun, D., L. Saleh, R. Garcia-Serres, B. M. Chicalese, Y. H. An, B. H. Huynh, and J. M. Bollinger, Jr. Addition of oxygen to the Diiron(II/II) cluster is the slowest step in formation of the tyrosyl radical in the W 103Y variant of ribonucleotide reductase protein R2 from mouse. Biochemistry 46:13067-13073. Mitic, N., M. D. Clay, L. Saleh, J. M. Bollinger, Jr., and E. I. Solomon. Spectroscopic and electronic-structure studies of intermediate X in ribonucleotide reductase R2 and two variants: A description of the FeIV-Oxo bond in the FeIII-O-FeIV dimer. J. Am. Chem. Soc. 129:9049-9065. Yun, D., R. Garcia-Serres, B. M. Chicalese, Y. H. An, B. H. Huynh, and J. M. Bollinger, Jr. A μ-1,2-peroxodiiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X, in assembly of the iron-radical cofactor of ribonucleotide reductase from mouse. Biochemistry 46:1925-1932. 2006 Hoffart, L. M., E. W. Barr, R. B. Guyer, J. M. Bollinger, Jr., and C. Krebs. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a Prolyl-4-hydroxylase. Proc. Natl. Acad. Sci. USA 103:14738-14743. Saleh, L. and J. M. Bollinger, Jr. Cation mediation of radical transfer between Trp48 and Tyr356 during O2 activation by protein R2 of Escherichia coli ribonucleotide reductase: relevance to R1-R2 radical transfer in nucleotide reduction? Biochemistry 45:8823-8830. Kim, S. H., G. Xing, J. M. Bollinger, Jr., C. Krebs, and B. M. Hoffman. Demonstration by 2H ENDOR spectroscopy that myo-inositol binds via an alkoxide bridge to the mixed-valent diiron center of myo-inositol oxygenase. J. Am. Chem. Soc. 128:10374-10375. Yeh, E., L. J. Cole, E. W. Barr, J. M. Bollinger, Jr., D. B. Ballou, and C. T. Walsh. Flavin redox chemistry precedes substrate chlorination during reaction of the flavin-dependent halogenase RebH. Biochemistry 45:7904-7912. Xing, G., Y. Diao, L. M. Hoffart, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr. Novel mechanisms of oxygen activation and C-H cleavage by a dinuclear iron cluster in myo-inositol oxygenase. Proc. Natl. Acad. Sci. USA 103:6130-6135. Xing, G., L. M. Hoffart, Y. Diao, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr. Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol-cleavage reaction catalyzed by myo-inositol oxygenase. Biochemistry 45:5402-5412. Xing, G., L. M. Hoffart, Y. Diao, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr. Spectroscopic evidence for a coupled dinuclear iron cluster that coordinates the substrate in myo-inositol oxygenase. Biochemistry 45:5393-5401. Bollinger, J. M., Jr. and C. Krebs. Stalking intermediates in oxygen activation by iron enzymes: Motivation and method. J. Inorg. Biochem. 100:586-605 2005 Bollinger, J. M. Jr., J. C. Price, L. M. Hoffart, E. W. Barr, and C. Krebs. Mechanism of taurine: a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Eur. J. Inorg. Chem. 21:4245-4254. Sommerhalter, M., L. Saleh, J.M. Bollinger, Jr., and A. C. Rosenzweig. Structure of Escherichia coli ribonucleotide reductase R2 in space group P6(1)22. Acta Cryst. D61:1649-1654. Price, J. C., E. W. Barr, L. M. Hoffart, C. Krebs, and J.M. Bollinger, Jr. Kinetic dissection of the catalytic mechanism of taurine: a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 44:8138-8147. Krebs, C., J. C. Price, J. Baldwin, L. Saleh, M. T. Green, and J.M. Bollinger, Jr. Rapid freeze-quench57Fe-Mössbauer spectroscopy: Monitoring changes of an iron-containing active site during a biochemical reaction. Inorg. Chem. 44:742-757. Shen, G., R. Balasubramanian, T. Wang, B. Tirupati, J.M. Bollinger, Jr., J. H. Golbeck, and D. A. Bryant. Functional genomics of genes for biogenesis of Fe-S proteins in cyanobacteria. In: Photosynthesis: Fundamental Aspects to Global Perspectives, Proceedings of the XIIIth International Congress on Photosynthesis, Montreal. (A. van der Est and D. Bruce, eds.), pp. 882-884, Allen Press, Lawrence, KA. 2004 Saleh, L., B.A. Kelch, B.A. Pathickal, J. Baldwin, B.A. Ley, and J.M. Bollinger, Jr. Mediation by indole analogues of electron transfer during oxygen activation in variants of Escherichia coli ribonucleotide reductase R2 lacking the electron-shuttling tryptophan 48. Biochemistry 43:5943-5952. Saleh, L., C. Krebs, B.A. Ley, S. Naik, B.H. Huynh, and J.M. Bollinger, Jr. Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase. Biochemistry 43:5953-5964. Wei, P.-p., A.J. Skulan, N. Mitic, Y.-S. Yang, L. Saleh, J.M. Bollinger, Jr., and E.I. Solomon. Electronic and spectroscopic studies of the non-heme reduced binuclear iron sites of two ribonucleotide reductase variants: comparison to reduced methane monooxygenase and contributions to O₂ reactivity. J. Am. Chem. Soc. 126:3777-3788. Behshad, E., S.E. Parkin, and J.M. Bollinger, Jr. Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: kinetic analysis of cleavage of the persulfide intermediate by chemical reductants. Biochemistry 43:12220-12226. Tirupati, B., J.L. Vey, C.L. Drennan, and J.M. Bollinger, Jr. Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803. Biochemistry 43:12210-12219. Lu, S., E. Libby, L. Saleh, G. Xing, J.M. Bollinger, Jr., and P. Moenne-Loccoz. Characterization of NO adducts of the diiron center in protein R2 of Escherichia coli ribonucleotide reductase and site-directed variants; implications for the O₂ activation mechanism. J. Biol. Inorg. Chem. 9:818-827. Skulan, A.J., T.C. Brunold, J. Baldwin, L. Saleh, J.M. Bollinger, Jr., and E.I. Solomon. Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant: implication for O₂ activation by binuclear non-heme iron enzymes. J. Am. Chem. Soc. 126:8842-8855. Riggs-Gelasco, P.J., J.C. Price, R.B. Guyer, J.H. Brehm, E.W. Barr, J.M. Bollinger, Jr., and C. Krebs. EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by Taurine:a-ketoglutarate dioxygenase. J. Am. Chem. Soc. 126:8108-8109. 2003 Baldwin, J., C. Krebs, L. Saleh, M. Stelling, B.H. Huynh, J.M. Bollinger, Jr., and P. Riggs-Gelasco. Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli. Biochemistry 42:13269-13279. Voegtli, W.C., M. Sommerhalter, L. Saleh, J. Baldwin, J.M. Bollinger, Jr., and A.C. Rosenzweig. Variable coordination geometries at the diiron(II) active site of ribonucleotide reductase R2. J. Am. Chem. Soc. 125:15822-15830. Price, J.C., E.W. Barr, B. Tirupati, J.M. Bollinger, Jr., and C. Krebs. The first direct characterization of a high-valent iron intermediate in the reaction of an a-ketoglutarate-dependent dioxygenase: A high-dpin Fe(IV) complex in taurine/a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42:7497-7508. Mitic, N., L. Saleh, G. Schenk, J.M. Bollinger, Jr., and E.I. Solomon. Rapid-freeze-quench magnetic circular dichroism of intermediate X in ribonucleotide reductase: new structural insight. J. Am. Chem. Soc. 125:11200-11201. Price, J.C., E.W. Barr, T.E. Glass, C. Krebs, and J.M. Bollinger, Jr. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine: a-ketoglutarate dioxygenase (TauD). J. Am. Chem. Soc. 125:13008-13009. 2002 Yun, D., 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. 41:981-990. Krebs, C., J.M. Bollinger, Jr., E.C. Thiel, and B.H. Huynh. Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy. J. Biol. Inorg. Chem. 7:863-869. 2001 Yun, D., 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 protien R2 of ribonucleotide reductase from mouse. Biochemistry. 41:981-990. Baldwin, J., W.C. Voegtli, N. Khidekel, P. Moenne-Loccoz, C. Krebs, A.S. Pereira, B.A. Ley, B.H. Huynh, T.M. Loehr, P.J. Riggs-Gelasco, A.C. Rosenzweig, and J.M. Bollinger, Jr. Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase. J. Am. Chem. Soc. 123:7017-7030. 2000 Voegtli, W.C., N. Khidekel, J. Baldwin, B.A. Ley, J.M. Bollinger, Jr., and A.C. Rosenzweig. Crystal Structure of the Ribonucleotide Reductase R2 Mutant that Accumulates a m-1,2-peroxodiiron(III) Intermediate During Oxygen Activation. J. Am. Chem. Soc. 122:3255-3261. Krebs, C., R. Davydov, J. Baldwin, B.M. Hoffman, J.M. Bollinger, Jr., and B.H. Huynh. Mössbauer and EPR Characterization of the S = 9/2 Mixed-valence Fe(II)Fe(III) Cluster in Cryoreduced R2 Subunit of Escherichia coli Ribonucleotide Reductase. J. Am. Chem. Soc. 122:5327-5336. Yang, Y.-S., J. Baldwin, B.A. Ley, J.M. Bollinger, Jr., and E.I. Solomon. Spectroscopic and Electronic Structure Description of the Reduced Binuclear Non-heme Iron Active Site in Ribonucleotide Reductase from E. coli: Comparison to Reduced D9 Desaturase and Electronic Structure Contributions to Differences in O2 Reactivity. J. Am. Chem. Soc. 122:8495-8510. Baldwin, J., C. Krebs, B.A. Ley, 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. 122:12195-12206. Krebs, C., S. Chen, J. Baldwin, B.A. Ley, U. Patel, 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. 2. Evidence for and Consequences of Blocked Electron Transfer in the W48F Variant. J. Am. Chem. Soc. 122:12207-12219. 1998 Bollinger, J.M., Jr., C. Krebs, A. Vicol, S. Chen, B.A. Ley, D.E. Edmondson, and B.H. Huynh. Engineering the Diiron Site of Escherichia coli Ribonucleotide Reductase Protein R2 to Accumulate an Intermediate Similar to Hperoxo, the Putative Peroxodiiron(III) Complex from the Methane Monooxygenase Catalytic Cycle. J. Am. Chem. Soc. 120:1094-1095. Huynh, B.H., J.M. Bollinger, Jr., and D.E. Edmondson. Reaction Intermediates in Oxygen Activation by Enzymes Containing Carboxylate-bridged Binuclear Iron Clusters. In: Spectroscopic Methods in Bioinorganic Chemistry. (E. I. Solomon and K. O. Hodgson, eds.), pp. 403-422, American Chemical Society, Washington, D.C. Moënne-Loccoz, P., J. Baldwin, B.A. Ley, T.M. Loehr, and J.M. Bollinger, Jr. O₂ Activation by Non-heme Diiron Proteins: Identification of a Symmetric m-1,2-peroxide in a Mutant of Ribonucleotide Reductase. Biochemistry. 37:14659-14663. Parkin, S.E., S. Chen, B.A. Ley, L. Mangravite, D.E. Edmondson, B.H. Huynh, and J.M. Bollinger, Jr. Electron Injection Through a Specific Pathway Determines the Outcome of Oxygen Activation at the Diiron Cluster in the F208Y Mutant of Escherichia coli Ribonucleotide Reductase Protein R2. Biochemistry. 37:1124-1130. 1997 J.M. Bollinger, Jr., C. Krebs, A. Vicol, S. Chen, B.A. Ley, D.E. Edmondson, and B.H. Huynh. Engineering the Diiron Site of Escherichia coli Ribonucleotide Reductase Protein R2 to Accumulate an Intermediate Similar to H_peroxo, the Putative Peroxodiiron (III) Complex from the Methane Monooxygenase Catalytic Cycle. J. Am. Chem. Soc. 120:1094-1095. D.S. Kwon, C.-H. Lin, S. Chen, J.K. Coward, C.T. Walsh, and J.M. Bollinger, Jr. Dissection of Glutathionylspermidine Synthetase/Amidase from Escherichia coli into Autonomously Folding and Functional Synthetase and Amidase Domains. J. Biol. Chem. 272:2429-2436. Lin, C.-H., D.S. Kwon, J.M. Bollinger, Jr., and C.T. Walsh. Evidence for a Glutathionyl-Enzyme Intermediate in the Amidase Activity of The Bifunctional Glutathionylspermidine Synthetase/Amidase from Escherichia coli. Biochemistry. 36:14930-14938. Parkin, S.E., S. Chen, B.A. Ley, L. Mangravite, D.E. Edmondson, B.H. Huynh, and J.M. Bollinger, Jr. Electron Injection through a Specific Pathway Determines the Outcome of Oxygen Activation at the Diiron Cluster in the F208Y Mutant of Escherichia coli Ribonucleotide Reductase Protein R2. Biochemistry. 37:1124-1130. 1995 Bollinger, J.M., Jr., D.S. Kwon, G.W. Huisman, R. Kolter, and C.T. Walsh. Glutathionylspermidine Metabolism in E. coli: Purification, Cloning, Overproduction and Characterization of a Bifunctional Glutathionylspermidine Synthetase/Amidase. J. Biol. Chem. 270:l403l-l404l. Bollinger, J.M., Jr., W.H. Tong, N. Ravi, B.H. Huynh, D.E. Edmondson, and J. Stubbe. Use of Rapid Kinetics Methods to Study the Assembly of the Diferric-Tyrosyl Radical Cofactor of E. coli Ribonucleotide Reductase. Methods Enzymol. 258:278-303. Hidalgo, E., J.M. Bollinger, Jr., T.M. Bradley, C.T. Walsh, B. Demple. Binuclear FeS Centers in the Escherichia coli SoxR Protein and Role of the Metal Centers in Transcription. J. Biol. Chem. 270:20908-209l4. Pulver, S.C., W.H. Tong, J.M. Bollinger, Jr., J. Stubbe, and E.I. Solomon. Circular Dichroism and Magnetic Circular Dichroism Studies of the Fully Reduced Binuclear Non-Heme Iron Active Site in the Escherichia coli R2 Subunit of Ribonucleoside Diphosphate Reductase. J. Am. Chem. Soc. ll7:l2664-l2687.
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