Selected Publications

Nemeria NS, Arjunan P, Chandrasekhar K, Mossad M, Tittmann K, Furey W, Jordan F. (2010) Communication between thiamin cofactors in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers: evidence for a "direct pathway" between the 4'-aminopyrimidine N1' atoms. J Biol Chem. 285(15):11197-209.

Song J, Park YH, Nemeria NS, Kale S, Kakalis L, Jordan F. (2010) Nuclear magnetic resonance evidence for the role of the flexible regions of the E1 component of the pyruvate dehydrogenase complex from gram-negative bacteria. J Biol Chem. 85(7):4680-94.

Jordan F, Arjunan P, Kale S, Nemeria NS, Furey W. (2009) Multiple roles of mobile active center loops in the E1 component of the Escherichia coli pyruvate dehydrogenase complex - Linkage of protein dynamics to catalysis. J Mol Catal B Enzym. 61(1-2):14-22.

Kale S, Jordan F. (2009) Conformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex. J Biol Chem. 284(48):33122-9.

Nemeria NS, Chakraborty S, Balakrishnan A, Jordan F. (2009) Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps. FEBS J. 276(9):2432-46.

Brandt GS, Kneen MM, Chakraborty S, Baykal AT, Nemeria N, Yep A, Ruby DI, Petsko GA, Kenyon GL, McLeish MJ, Jordan F, Ringe D. (2009) Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor. Biochemistry. 48(15):3247-57.

Chakraborty S, Nemeria NS, Balakrishnan A, Brandt GS, Kneen MM, Yep A, McLeish MJ, Kenyon GL, Petsko GA, Ringe D, Jordan F. (2009) Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. Biochemistry. 48(5):981-94.

Brandt GS, Nemeria N, Chakraborty S, McLeish MJ, Yep A, Kenyon GL, Petsko GA, Jordan F, Ringe D. (2008) Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester. Biochemistry. 47(29):7734-43.

Chakraborty S, Nemeria N, Yep A, McLeish MJ, Kenyon GL, Jordan F. (2008) Mechanism of benzaldehyde lyase studied via thiamin diphosphate- bound intermediates and kinetic isotope effects. Biochemistry. 47(12):3800-9.

Kale S, Ulas G, Song J, Brudvig GW, Furey W, Jordan F. (2008) Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex. Proc Natl Acad Sci U S A. 105(4):1158-63.

Nemeria N, Korotchkina L, McLeish MJ, Kenyon GL, Patel MS, Jordan F. (2007) Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states. Biochemistry. 46(37):10739-44.

Kale S, Arjunan P, Furey W, Jordan F. (2007) A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. J Biol Chem. 282(38):28106-16.

Jordan F. (2007) Adenosine triphosphate and thiamine cross paths. Nat Chem Biol. 3(4):202-3.

Schweitzer-Stenner R, Measey T, Kakalis L, Jordan F, Pizzanelli S, Forte C, Griebenow K. (2007) Conformations of alanine-based peptides in water probed by FTIR, Raman, vibrational circular dichroism, electronic circular dichroism, and NMR spectroscopy. Biochemistry. F46(6):1587-96.

Nemeria N, Chakraborty S, Baykal A, Korotchkina LG, Patel MS, Jordan F. (2007) The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proc Natl Acad Sci U S A. 104(1):78-82.

Joseph E, Wei W, Tittmann K, Jordan F. (2006) Function of a conserved loop of the beta-domain, not involved in thiamin diphosphate binding, in catalysis and substrate activation in yeast pyruvate decarboxylase. Biochemistry. 45(45):13517-27.

Baykal AT. Kakalis L. Jordan F. (2006) Electronic and nuclear magnetic resonance spectroscopic features of the 1',4'-iminopyrimidine tautomeric form of thiamin diphosphate. a novel intermediate on enzymes requiring this coenzyme. Biochemistry. 45(24):7522-8.

Arjunan P. Sax M. Brunskill A. Chandrasekhar K. Nemeria N. Zhang S. Jordan F. Furey W. (2006) A thiamin-bound. pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. J Biol Chem. 281(22):15296-303.

Jordan F. Nemeria NS. Sergienko E. (2005) Multiple modes of active center communication in thiamin diphosphate-dependent enzymes. Acc Chem Res. 38(9):755-63.

Jordan F. Nemeria NS. (2005) Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations. Bioorg Chem. 33(3):190-215.

Nemeria N. Tittmann K. Joseph E. Zhou L. Vazquez-Coll MB. Arjunan P. Hubner G. Furey W. Jordan F.
(2005) Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity. J Biol Chem. 280(22):21473-82.

Zhang S. Zhou L. Nemeria N. Yan Y. Zhang Z. Zou Y. Jordan F. (2005) Evidence for dramatic acceleration of a C-H bond ionization rate in thiamin diphosphate enzymes by the protein environment. Biochemistry. 44(7):2237-43.

Park YH. Wei W. Zhou L. Nemeria N. Jordan F. (2004) Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit. Biochemistry. 43(44):14037-46.

Jordan F. (2004) Biochemistry. How active sites communicate in thiamine enzymes. Science. 306(5697):818-20.

Zhang S. Liu M. Yan Y. Zhang Z. Jordan F. (2004) C2-alpha-lactylthiamin diphosphate is an intermediate on the pathway of thiamin diphosphate-dependent pyruvate decarboxylation. Evidence on enzymes and models. J Biol Chem. 279(52):54312-8.

Nemeria N. Baykal A. Joseph E. Zhang S. Yan Y. Furey W. Jordan F. (2004) Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme. unlike the michaelis complex or the free coenzyme. Biochemistry. 43(21):6565-75.

Arjunan P. Chandrasekhar K. Sax M. Brunskill A. Nemeria N. Jordan F. Furey W. (2004) Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate. Biochemistry. 43(9):2405-11.

Jordan F. Nemeria NS. Zhang S. Yan Y. Arjunan P. Furey W. (2003) Dual catalytic apparatus of the thiamin diphosphate coenzyme: acid-base via the 1',4'-iminopyrimidine tautomer along with its electrophilic role. J Am Chem Soc. 125(42):12732-8.

Tittmann K. Golbik R. Uhlemann K. Khailova L. Schneider G. Patel M. Jordan F. Chipman DM. Duggleby RG. Hubner G. (2003) NMR analysis of covalent intermediates in thiamin diphosphate enzymes. Biochemistry. 42(26):7885-91.

Jordan F. (2003) Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions. Nat Prod Rep. 20(2):184-201.

Wei W. Li H. Nemeria N. Jordan F. (2003) Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase. Protein Expr Purif. 28(1):140-50.

Polovnikova ES. McLeish MJ. Sergienko EA. Burgner JT. Anderson NL. Bera AK. Jordan F. Kenyon GL. Hasson MS. (2003) Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme. benzoylformate decarboxylase. Biochemistry. 42(7):1820-30.

Arjunan. P.. Nemeria. N.. Brunskill. A.. Chandrasekhar. K.. Sax. M.. Yan. Y.. Jordan. F.. Guest J.R. and Furey. W. (2002)Structure of the pyruvate dehydrogenase multienzyme complex E1 Component from E. coli at 1.85 Å resolution. Biochemistry. 41(16):5213-21.

Sergienko. E.A.. and Jordan. F. (2002) Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants. with substitution of adjacent active center acidic groups from different subunits. display restored activity. Biochemistry. 41(19):6164-9.

Wei. W.. Min Liu. M. and Jordan. F. (2002) Solvent kinetic isotope effects monitor changes in hydrogen bonding at the active center of yeast pyruvate decarboxylase concomitant with substrate activation. The substituent at Position 221 can control the state of activation. Biochemistry 41:451-461.

Kahyaoglu. A. and Jordan. F. (2002) Direct proton magnetic resonance determination of the pKa of the active center histidine in thiolsubtilisin. Protein Science 11:965-973.

Sergienko E. A. and Jordan. F. (2002) A new model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: Demonstration of the existence of two active forms of the enzyme. Biochemistry 41:3952-3967.