Professor

Contact Info

Office:
511
Phone Number:
Lab Office:
528,530,532
Personal Website:
Research Interests:

Enzymes are remarkable biocatalysts, not only for the dramatic rate accelerations (up to 1020 fold) that they provide, but also for the high degree of substrate specificity, regiospecificity and stereospecificity that these reactions exhibit. The work in my laboratory is focused on the chemical basis for how enzymes achieve such high rates and reaction specificity. Two groups of enzymes are currently under study in the laboratory: 1) Pyridoxal 5'-phosphate (PLP; vitamin B6) dependent enzymes, and, 2) Alcohol dehydrogenases. Tyrosine phenol-lyase and tryptophan indole-lyase are two PLP-dependent enzymes that catalyze the hydrolytic cleavage of tyrosine or tryptophan to phenol or indole, respectively, and ammonium pyruvate. Although the amino acid sequences and three dimensional structures of the two enzymes are very similar, these enzyme are specific for their physiological substrates. We are determining the chemical mechanisms of both enzymes by synthesis of substrate and transition state analogs, steady state and rapid-scanning stopped-flow kinetics, and by using site-directed mutagenesis. We are also altering the substrate specificity by mutagenesis to identify the amino acids which determine the reaction specificity. Another PLP-dependent enzyme being studied in my laboratory is kynureninase. We have cloned this enzyme from Pseudomonas fluorescens and Homo sapiens and we have studied the mechanism by steady state and pre-steady state kinetic methods. Recently, we have determined the crystal structures of bacterial and human kynureninases, and we are determining the structural basis for the differences in reaction specificity. We have also synthesized potent mechanism based inhibitors of kynureninase that could be useful as drugs. In other work, we are studying a thermostable secondary alcohol dehydrogenase (SADH) isolated from a thermophilic bacterium. We demonstrated a novel temperature dependent reversal of stereospecificity of SADH in the reaction of 2-butanol. We are currently investigating a mutant SADH with specificity for aromatic substrates. A new project uses hydrostatic pressure as a probe of conformational changes in enzymes and proteins.  (This research was partially supported by a grant from the National Institutes of Health and the National Science Foundation.)

Selected Publications:

2011-2018

Phillips, R. S., Ting, S. C., Tetsadjio, A. G., Anderson, K. L., Friez, K. M., Miller, K. A., & Hoover, T. R. (2017). Properties and mechanism of d-glucosaminate-6-phosphate ammonia-lyase: An aminotransferase family enzyme with d-amino acid specificity.. Biochim Biophys Acta. doi:10.1016/j.bbapap.2017.12.006

Rossignoli, G., Phillips, R. S., Astegno, A., Menegazzi, M., Voltattorni, C. B., & Bertoldi, M. (n.d.). Phosphorylation of pyridoxal 5'-phosphate enzymes: an intriguing and neglected topic.. Amino Acids, 50(2), 205-215. doi:10.1007/s00726-017-2521-3

Barbolina, M. V., Kulikova, V. V., Tsvetikova, M. A., Anufrieva, N. V., Revtovich, S. V., Phillips, R. S., . . . Faleev, N. G. (2017). Serine 51 residue of Citrobacter freundii tyrosine phenol-lyase assists in C-α-proton abstraction and transfer in the reaction with substrate.. Biochimie. doi:10.1016/j.biochi.2017.11.016

Phillips, R. S., Poteh, P., Miller, K. A., & Hoover, T. R. (2017). STM2360 encodes a d -ornithine/ d -lysine decarboxylase in Salmonella enterica serovar typhimurium. Archives of Biochemistry and Biophysics, 634, 83-87. doi:10.1016/j.abb.2017.09.010

Nealon, C. M., Kim, C. S., Dwamena, A. K., & Phillips, R. S. (2017). Mutagenesis of Met-151 and Thr-153 to alanine in Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase changes substrate specificity for acetophenones. Enzyme and Microbial Technology, 105, 59-63. doi:10.1016/j.enzmictec.2017.06.010

Phillips, R. S. (2017). Chapter 24:  The Kynurenine Pathway of Tryptophan Metabolism in Microorganisms. In F. D'Mello (Ed.), The Handbook of Microbial Metabolism of Amino Acids. UK: Cabi.

Gogal, R. G., Bringolf, R., Philips, R., Guo, T. L., & Holladay, S. D. (2017). Anesthetic activity of acetylated MS-222 in tilapia (Oreochromis niloticus). GSTF Journal of Veterinary Science, 4, 1-6.

Phillips, R. S. (2016). Ground-state Destabilization in Pyridoxal-5'-phosphate Dependent Enzymes:  Tyrosine Phenol-lyase and Tryptophan Indole-lyase. In 5th Congress of the Russian Biochemical Society. Sochi, Russia.

Phillips, R. S., Vita, A., Spivey, J. B., Rudloff, A. P., Driscoll, M. D., & Hay, S. (2016). Ground-State Destabilization by Phe-448 and Phe-449 Contributes to Tyrosine Phenol-Lyase Catalysis. ACS CATALYSIS, 6(10), 6770-6779. doi:10.1021/acscatal.6b01495

Phillips, R. S. (2016). Ground-state Destabilization in Pyridoxal-5'-phosphate Dependent Enzymes. In 5th International Meeting on Cofactors and Coenzymes. Kurobe, Japan.

Nealon, C. M., Welsh, T. P., Kim, C. S., & Phillips, R. S. (2016). I86A/C295A mutant secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus has broadened substrate specificity for aryl ketones. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 606, 151-156. doi:10.1016/j.abb.2016.08.002

Phillips, R. S. (2016). Structure of the Tryptophan Indole-lyase-Oxindolylalanine Complex. In Fifth International Symposium on Diffraction Structural Biology. Knoxville, TN.

Phillips, R. S. (2016). Phosphorylation of PLP-dependent Enzymes. In Department of Biochemistry, University of Verona. Verona, Italy.

Phillips, R. S. (2016). Ground-state destabilization in PLP catalysis:  Tyrosine phenol-lyase and tryptophan indole-lyase. In Department of Biochemistry, University of Verona. Verona, Italy.

Phillips, R. S. (2016). Ground-state destabilization in PLP catalysis:  Tyrosine phenol-lyase and tryptophan indole-lyase. In Department of Biochemistry, University of Parma. Parma, Italy.

Do, Q., Nguyen, G. T., & Phillips, R. S. (2016). Inhibition of tyrosine phenol-lyase by tyrosine homologues. AMINO ACIDS, 48(9), 2243-2251. doi:10.1007/s00726-016-2263-7

Phillips, R. S., Anderson, A. D., Gentry, H., Bowen, J. P., & Guner, O. (2016). Inhibition Studies of Kynurenine 3-Monoxygenase with Potential Applications to Neurodegenerative Disorders. In 7th Southeast Enzyme Conference. Atlanta, Georgia State University, GA..

Phillips, R. S., Vita, A., Spivey, J. B., Rudloff, A. P., Driscoll, M. D., & Hay, S. (2016). Ground-state Destabilization by Phe-448 and Phe-449 in Tyrosine Phenol-lyase Catalysis. In 7th Southeast Enzyme Conference. Atlanta, Georgia State University, GA..

Phillips, R. S., Ting, S. C., Tetsadjio, A., Miller, K. A., Hoover, T. R., Momany, C., & Galloway, N. R. (2016). Glucosaminate 6-phosphate Ammonia Lyase from Salmonella typhimurium:  A Novel Pyridoxal-5'-phosphate Dependent Enzyme. In 7th Southeast Enzyme Conference. Atlanta, Georgia State University, GA..

Phillips, R. S., Crocker, M., & Idowu, O. E. (2016). Effects of Kynurenine and Benzoyl-L-alanine with S36A Pseudomonas fluorescens Kynureninase. In 7th Southeast Enzyme Conference. Atlanta, Georgia State University, GA.

Phillips, R. S., Anderson, A. D., Gentry, H. G., Guner, O. F., & Bowen, J. P. (2017). Substrate and inhibitor specificity of kynurenine monooxygenase from Cytophaga hutchinsonii. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 27(8), 1705-1708. doi:10.1016/j.bmcl.2017.02.080

Phillips, R. S., Gogal, R. M., Bringolf, R., Guo, T. L., & Holladay, S. (2016). Anesthetic activity of acetylated MS-222 in tilapia (Oreochromis niloticus). J. Aquat. Anim. Health..

Phillips, R. S. (2015). Chemistry and diversity of pyridoxal-5 '-phosphate dependent enzymes. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1854(9), 1167-1174. doi:10.1016/j.bbapap.2014.12.028

Miller, K. A., Phillips, R. S., Kilgore, P. B., Smith, G. L., & Hoover, T. R. (2015). A Mannose Family Phosphotransferase System Permease and Associated Enzymes Are Required for Utilization of Fructoselysine and Glucoselysine in Salmonella enterica Serovar Typhimurium. JOURNAL OF BACTERIOLOGY, 197(17), 2831-2839. doi:10.1128/JB.00339-15

Phillips, R. S., Maitrani, C., Guner, O. F., Anderson, A. D., Gentry, H. G., & Bowen, J. P. (2015). Substrate and inhibitor specificity of kynurenine monooxygenase and kynureninase. AMINO ACIDS, 47(8), 1635. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000358175100080&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Musa, M. M., Patel, J. M., Nealon, C. M., Kim, C. S., Phillips, R. S., & Karume, I. (2015). Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase mutants with improved racemization activity. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 115, 155-159. doi:10.1016/j.molcatb.2015.02.012

Nealon, C. M., Musa, M. M., Patel, J. M., & Phillips, R. S. (2015). Controlling Substrate Specificity and Stereospecificity of Alcohol Dehydrogenases. ACS CATALYSIS, 5(4), 2100-2114. doi:10.1021/cs501457v

Kadirvelraj, R., Sennett, N. C., Custer, G. S., Phillips, R. S., & Wood, Z. A. (2015). Hysteresis and Negative Cooperativity in Human UDP-Glucose Dehydrogenase (vol 52, pg 1456, 2013). BIOCHEMISTRY, 54(2), 629. doi:10.1021/bi501527p

Phillips, R. S., Demidkina, T. V., & Faleev, N. G. (2014). The role of substrate strain in the mechanism of the carbon-carbon lyases. BIOORGANIC CHEMISTRY, 57, 198-205. doi:10.1016/j.bioorg.2014.06.002

Do, Q. T., Nguyen, G. T., Celis, V., & Phillips, R. S. (2014). Inhibition of Escherichia coli tryptophan indole-lyase by tryptophan homologues. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 560, 20-26. doi:10.1016/j.abb.2014.07.027

Faleev, N. G., Zakomirdina, L. N., Vorob'ev, M. M., Tsvetikova, M. A., Gogoleva, O. I., Demidkina, T. V., & Phillips, R. S. (2014). A straightforward kinetic evidence for coexistence of "induced fit" and "selected fit" in the reaction mechanism of a mutant tryptophan indole lyase Y72F from Proteus vulgaris. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1844(10), 1860-1867. doi:10.1016/j.bbapap.2014.07.014

Venkatesh, M., Mukherjee, S., Wang, H., Li, H., Sun, K., Benechet, A. P., . . . Mani, S. (2014). Symbiotic Bacterial Metabolites Regulate Gastrointestinal Barrier Function via the Xenobiotic Sensor PXR and Toll-like Receptor 4. IMMUNITY, 41(2), 296-310. doi:10.1016/j.immuni.2014.06.014

Patel, J. M., Musa, M. M., Rodriguez, L., Sutton, D. A., Popik, V. V., & Phillips, R. S. (2014). Mutation of Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase at Trp-110 affects stereoselectivity of aromatic ketone reduction. ORGANIC & BIOMOLECULAR CHEMISTRY, 12(31), 5905-5910. doi:10.1039/c4ob00794h

Phillips, R. S. (2014). Structure and mechanism of kynureninase. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 544, 69-74. doi:10.1016/j.abb.2013.10.020

Phillips, R. S., Scott, I., Paulose, R., Patel, A., & Barron, T. C. (2014). The phosphate of pyridoxal-5 '-phosphate is an acid/base catalyst in the mechanism of Pseudomonas fluorescens kynureninase. FEBS JOURNAL, 281(4), 1100-1109. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000331453600009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Patel, J. M., & Phillips, R. S. (2014). Effects of Hydrostatic Pressure on Stereospecificity of Secondary Alcohol Dehydrogenase from Thermoanaerobacter Ethanolicus Support the Role of Solvation in Enantiospecificity. ACS CATALYSIS, 4(2), 692-694. doi:10.1021/cs4010997

Maitrani, C., & Phillips, R. S. (2013). Substituents effects on activity of kynureninase from Homo sapiens and Pseudomonas fluorescens. BIOORGANIC & MEDICINAL CHEMISTRY, 21(15), 4670-4677. doi:10.1016/j.bmc.2013.05.039

Phillips, R. S. (2013). Structural basis of the substrate specificity of human and bacterial kynureninase. In FEBS JOURNAL Vol. 280 (pp. 171-172). Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000325919201043&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Harris, A. P., & Phillips, R. S. (2013). Benzimidazole analogs of L-tryptophan are substrates and inhibitors of tryptophan indole lyase from Escherichia coli. FEBS JOURNAL, 280(8), 1807-1817. doi:10.1111/febs.12205

Phillips, R. S., Busby, S., Edenfield, L., & Wickware, K. (2013). Preparation of 3-bromo-L-tyrosine and 3,5-dibromo-L-tyrosine. AMINO ACIDS, 44(2), 529-532. doi:10.1007/s00726-012-1366-z

Kadirvelraj, R., Sennett, N. C., Custer, G. S., Phillips, R. S., & Wood, Z. A. (2013). Hysteresis and Negative Cooperativity in Human UDP-Glucose Dehydrogenase. BIOCHEMISTRY, 52(8), 1456-1465. doi:10.1021/bi301593c

Musa, M. M., Phillips, R. S., Laivenieks, M., Vieille, C., Takahashi, M., & Hamdan, S. M. (2013). Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase. ORGANIC & BIOMOLECULAR CHEMISTRY, 11(17), 2911-2915. doi:10.1039/c3ob27415b

Phillips, R. S., Wang, A. K., Marchal, S., & Lange, R. (2012). Effects of Pressure and Osmolytes on the Allosteric Equilibria of Salmonella typhimurium Tryptophan Synthase. BIOCHEMISTRY, 51(46), 9354-9363. doi:10.1021/bi301002q

Phillips, R. S., Kalu, U., & Hay, S. (2012). Evidence of Preorganization in Quinonoid Intermediate Formation from L-Trp in H463F Mutant Escherichia coli Tryptophan Indole-lyase from Effects of Pressure and pH. BIOCHEMISTRY, 51(33), 6527-6533. doi:10.1021/bi300632k

Maitrani, C., Heyes, D. J., Hay, S., Arumugam, S., Popik, V. V., & Phillips, R. S. (2012). Preparation and photophysical properties of a caged kynurenine. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 22(8), 2734-2737. doi:10.1016/j.bmcl.2012.02.097

Do, Q. T., & Phillips, R. S. (2012). Bioconversion of glycerol surplus into L-tryptophan using tryptophan-indole lyase. In ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY Vol. 243. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000324475100795&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Mukherjee, S., Wang, H., Venkatesh, M., Maher, L., Kortagere, S., Phillips, R. S., . . . Mani, S. (2011). Epithelial expression of the orphan nuclear receptor PXR is critical for the maintenance of gut mucosal barrier function. INFLAMMATORY BOWEL DISEASES, 17, S11. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000297735300034&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Zhang, Y., Shen, J., He, X., Zhang, K., Wu, S., Xiao, B., . . . Zhu, D. (2011). A Rare Variant at the KYNU Gene Is Associated With Kynureninase Activity and Essential Hypertension in the Han Chinese Population. CIRCULATION-CARDIOVASCULAR GENETICS, 4(6), 687-U451. doi:10.1161/CIRCGENETICS.110.959064

Phillips, R. S. (2011). Structure, mechanism, and substrate specificity of kynureninase. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1814(11), 1481-1488. doi:10.1016/j.bbapap.2010.12.003

Milic, D., Demidkina, T. V., Faleev, N. G., Phillips, R. S., Matkovic-Calogovic, D., & Antson, A. A. (2011). Crystallographic Snapshots of Tyrosine Phenol-lyase Show That Substrate Strain Plays a Role in C-C Bond Cleavage. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 133(41), 16468-16476. doi:10.1021/ja203361g

Phillips, R. (2011). Hydrostatic Pressure As a Probe of Conformational Changes in PLP Enzymes. In 3rd International Conference on Coenzymes. Turku, Finland.

Phillips, R. (2011). Determining Mechanisms of PLP-Dependent Enzymes With Rapid-kinetic Techniques. University of Verona, Italy: Department of Biochemistry.

Phillips, R. (2011). Hydrostatic Pressure as a Probe of Conformational Changes in PLP-Dependent Enzymes. University of Parma, Italy: Department of Biochemistry.

Phillips, R. (2011). Design of I86A/C295A SADH for Chiral Reduction of Substituted Acetophenones. Milan, Italy: CNR.

Kumar, S., Gawandi, V., Capito, N., & Phillips, R. (2011). Substituent Effects on the Reaction of ß-Benzoylalanines with Pseudomonas fluorescens Kynureninase. In Second Southeast Enzyme Conference.

Phillips, R., & Do, Q. (2011). Enzymatic Synthesis of L-Tryptophan by E. coli Whole-Cells Catalysis from Indole, Glycerol and Ammonium Acetate. In Second Southeast Enzyme Conference. Georgia State University, Atlanta, GA.

Phillips, R. (2011). Tryptophan, the Chemical Behind your Turkey-induced Nap, and Human History. UGA: Willson Center for Humanities and Arts.

Phillips, R. S., Ghaffari, R., Dinh, P., Lima, S., & Bartlett, D. (2011). Properties of tryptophan indole-lyase from a piezophilic bacterium, Photobacterium profundum SS9. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 506(1), 35-41. doi:10.1016/j.abb.2010.11.002

Kumar, S., Gawandi, V., Capito, N., & Phillips, R. (2011). Substituent Effects on the Reaction of ß-Benzoylalanines with Pseudomonas fluorescens Kynureninase. In 22nd Enzyme Mechanisms Conference. St. Petersburg Beach, FL.

Musa, M. M., & Phillips, R. S. (2011). Recent advances in alcohol dehydrogenase-catalyzed asymmetric production of hydrophobic alcohols. CATALYSIS SCIENCE & TECHNOLOGY, 1(8), 1311-1323. doi:10.1039/c1cy00160d

Vila-Real, H., Alfaia, A. J., Calado, A. R., Phillips, R. S., & Ribeiro, M. H. L. (2011). High pressure: a tool to improve the enzymatic production of glycosides. HIGH PRESSURE RESEARCH, 31(3), 475-487. doi:10.1080/08957959.2011.596538

Amster, I. J., & Phillips, R. S. (2007, August 28). 7,951,602, Mass Defect Label For Cysteine And Methods Of Use Thereof.

Lima, S., Sundararaju, B., Huang, C., Khristoforov, R., Momany, C., & Phillips, R. S. (n.d.). The Crystal Structure of the Pseudomonas dacunhae Aspartate-ß-Decarboxylase. Retrieved from http://www.rcsb.org/pdb/explore.do?structureId=3FDD

Miller, K. A., Phillips, R. S., Mrazek, J., & Hoover, T. R. (2013). Salmonella Utilizes D-Glucosaminate via a Mannose Family Phosphotransferase System Permease and Associated Enzymes. JOURNAL OF BACTERIOLOGY, 195(18), 4057-4066. doi:10.1128/JB.00290-13

Phillips, R. S., Miles, E. W., McPhie, P., Marchal, S., Lange, R., Holtermann, G., & Goody, R. S. (2010). Effects of hydrostatic pressure on the conformational equilibrium of tryptophan synthase from Salmonella typhimurium. HIGH-PRESSURE BIOSCIENCE AND BIOTECHNOLOGY, 1189, 95-103. doi:10.1111/j.1749-6632.2009.05201.x

Lima, S., Gawandi, V., Momany, C., & Phillips, R. S. (2006). Crystal structure of the Homo sapiens kynureninase-2-amino-3-hydroxyhippuric acid inhibitor complex. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000236326200364&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

2010

Kumar, S. ; Gawandi, V. B. ; Capito, N. ; Phillips, R. S. Substituent effects on the reaction of beta-benzoylalanines with Pseudomonas fluorescens kynureninase. Biochemistry 2010, 49, 7913-9.

Phillips, R. S. ; Lima, S. ; Khristoforov, R. ; Sudararaju, B. Insights into the mechanism of Pseudomonas dacunhae aspartate beta-decarboxylase from rapid-scanning stopped-flow kinetics. Biochemistry 2010, 49, 5066-73.

2009

Marchal, S. ; Font, J. ; Ribó, M. ; Vilanova, M. ; Phillips, R. S. ; Lange, R. ; Torrent, J. Asymmetric kinetics of protein structural changes. Accounts of chemical research 2009, 42, 778-87.

Lima, S. ; Kumar, S. ; Gawandi, V. ; Momany, C. ; Phillips, R. S. Crystal structure of the Homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: insights into the molecular basis of kynureninase substrate specificity. Journal of medicinal chemistry 2009, 52, 389-96.

Lima, S. ; Sundararaju, B. ; Huang, C. ; Khristoforov, R. ; Momany, C. ; Phillips, R. S. The crystal structure of the Pseudomonas dacunhae aspartate-beta-decarboxylase dodecamer reveals an unknown oligomeric assembly for a pyridoxal-5'-phosphate-dependent enzyme. Journal of molecular biology 2009, 388, 98-108.

2008

Phillips, R. S. ; Miles, E. W. ; McPhie, P. ; Marchal, S. ; Georges, C. ; Dupont, Y. ; Lange, R. Pressure and temperature jump relaxation kinetics of the conformational change in Salmonella typhimurium tryptophan synthase L-serine complex: large activation compressibility and heat capacity changes demonstrate the contribution of solvation. Journal of the American Chemical Society 2008, 130, 13580-8.

Osborne, A. S. ; Som, P. ; Metcalf, J. L. ; Phillips, R. S. Regioselective nitration of N(alpha),N(1)-bis(trifluoroacetyl)-L-tryptophan methyl ester: efficient synthesis of 2-nitro and 6-nitro-N-trifluoroacetyl-L-tryptophan methyl ester. Bioorganic & medicinal chemistry letters 2008, 18, 5750-2.

Musa, M. M. ; Ziegelmann-Fjeld, K. I. ; Vieille, C. ; Phillips, R. S. Activity and selectivity of W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus in organic solvents and ionic liquids: mono- and biphasic media. Organic & biomolecular chemistry 2008, 6, 887-92.

2007

Song, L. ; Teng, Q. ; Phillips, R. S. ; Brewer, J. M. ; Summers, A. O. 19F-NMR reveals metal and operator-induced allostery in MerR. Journal of molecular biology 2007, 371, 79-92.

Musa, M. M. ; Ziegelmann-Fjeld, K. I. ; Vieille, C. ; Zeikus, G. J. ; Phillips, R. S. Xerogel-encapsulated W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus performs asymmetric reduction of hydrophobic ketones in organic solvents. Angewandte Chemie (International ed. in English) 2007, 46, 3091-4.