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Aimin Liu

                   Dr. Aimin Liu

                  Associate Professor
                  Department of Chemistry
                  Georgia State University
                  P.O. Box 4098
                  Atlanta, Georgia 30302-4098

                  Office: 608 Kell Hall
                  Phone: 404-413-5532
                  Email: Feradical@gsu.edu

 

 

 

Research Interest: 1) Role of Metals in Biology and Medicine; 2) Cellular Signaling and Transcriptional Regulation by Metalloproteins; 3) Mechanistic Enzymology and Metabolic Pathways; 4) Oxidative Stress and Free Radical in Cancer Biology; and 5) EPR Spectroscopy

The Liu Lab's research program lies at the interface of biochemistry, bioinorganic chemistry, spectroscopy, and cancer biology. The current ongoing research is directed towards understanding the interaction of metal ions in enzymes/proteins with other chemical and biological molecules. The Liu Lab's long term goal is to determine the chemical basis for the biological roles and physiological effects of metal ions and protein-based free radicals. At present, the Liu laboratory has three concurrent research foci. The first project concerns the molecular mechanism of signal transduction regulation. The Liu Lab employs a wide array of biochemical, biophysical, bioinformatics, molecular and cellular biology to study a nuclear metalloprotein that participates in cell signaling through modulation of the transactivation of inducible transcription factors such as NF-κB. The Liu Lab's second project concerns tryptophan metabolism and neuropsychiatric problems. The Liu Lab is engaged in studying mechanistic enzymology and regulation of tryptophan's kynurenine pathway. The chemical mechanism of tryptophan 2,3-dioxygenase (TDO) and α-amino-β-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD) of the kynurenine pathway are being elucidated by using biochemical and spectroscopic approaches. Additionally, the Liu Lab is also interested in the metalloenzymes involved in sulfur metabolism. The Liu Lab's third project is placed on radical enzymology, which studies free radicals produced during oxygen activation and protein-based radicals. These research activities are supported by grants and awards from NSF, Georgia Cancer Coalition, and GSU.

Academic Distinction:

2009  NSF Program Review Panelist
2009  Distinguished Cancer Scientient Award, The Georgia Cancer Coalition
2009  Principal Investigator, NSF Grant No. MCB-0843537
2009  Cleon F. Arrington Research Initiation Award, Georgia State University
2008  Visiting Professor at Kansai University (Japan)
2006  Steering Committee member, Neuroscience Graduate Curriculum, UMMC, Jackson, MS
2006  Temporary member of the MSFA Study Section, NIH
2005  NSF CHE & MCB proposal ad hoc reviewer
2003  Ralph E. Powe Junior Faculty Enhancement Award in Life Sciences, Oak Ridge Associated Universities (ORAU)
2002  Paul D. Boyer Award for Research Excellence, Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota
2002  Cyrus P. and Anne R. Barnum Travel Award, Minnesota Medical Foundation, Minneapolis, MN
1999  Wenner-Gren Center Foundation Travel Fellowship, Stockholm, Sweden
1997  Poster Presentation Award, Society of Chemical Industry (SCI), London, UK
1996  Royal Society K.C. Wong Fellowship, The Royal Society, London, UK
1995  National Prize for Promotion of Science and Technology from National Education Commission, Beijing, China
1993  Principal Investigator, Chinese National Science Foundation Research Grant, Beijing, China
1991  Presidential Award, Chinese Academy of Sciences (CAS), Beijing, China

Invited Seminars & Talks (since independent career):

11/2009  Georgia Institute of Technology
 09/2009   University of Florida
07/2009  14th International Conference on Biological Inorganic Chemistry (ICBIC14), Nagoya, Japan
08/2008  Auburn University
06/2008  Osaka University
05/2008  Tohoku University
05/2008  Kansai University
04/2008  The 235th National American Chemical Society Conference, New Orleans, LA
03/2008  University of Southern Mississippi
01/2008  Gordon Research Conferences (GRC) - Protein Cofactors, Radicals, and Quinones, Ventura, CA
10/2007  Pennsylvania State University
01/2006  Gordon Research Conferences (GRC) - Metals in Biology, Ventura, CA
01/2006  The Inaugural Texas Enzyme Mechanism Conference, Austin, TX
11/2003  Poster talk, Gordon Research Conferences (GRC) - Enzyme, Coenzyme & Metabolic Pathways
06/2003  Jackson State University - NIH-Sponsored SCORE Seminar Series
02/2003  Mississippi State University

Recent Peer-Reviewed Journal Articles (past ten years)

  1. Liu A, Pötsch S, Davydov A, Barra A, Rubin H, and Gräslund A (1998) The tyrosyl free radical of recombinant ribonucleotide reductase from Mycobacterium tuberculosis is located in a rigid hydrophobic pocket. Biochemistry 37(46), 16369-16377.    [Abstract]    [PDF]
  2. Liu A, Sahlin M, Pötsch S, Sjöberg BM, Gräslund A (1998) New paramagnetic species formed at the expense of the transient tyrosyl radical in mutant protein R2 F208Y of Escherichia coli ribonucleotide reductase. Biochem. Biophys. Res. Commun. 246(3), 740-745.    [Abstract]    [PDF]
  3. Zhou T and Liu A, Mo Y, and Zhang H (2000) Sequential mechanism of methane dehydrogenation over metal oxide and carbide catalysts. J. Phys. Chem. (A). 104(19), 4505-4513.    [Abstract]   [PDF]
  4. Liu A and Gräslund A (2000) EPR evidence for a novel interconversion of [3Fe-4S]+ and [4Fe-4S]+ clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activase in vitro. J. Biol. Chem. 275(17), 12367-12373.    [Abstract]   [PDF]
  5. Chabes A, Domkin V, Larsson G, Liu A, Gräslund A, Wijmenga S, and Thelander L (2000) Yeast ribonucleotide reductase - a new type of ribonucleotide reductase with a heterodimeric iron-radical containing subunit. Proc. Natl. Acad. Sci. U.S.A. 97, 2474-2479.    [Abstract]   [PDF]
  6. Liu A, Barra AL, Rubin H, Lu G, and Gräslund A (2000) Heterogeneity of the local electrostatic environment of the tyrosyl radical in Mycobacterium tuberculosisribonucleotide reductase observed by high-field EPR spectroscopy. J. Am. Chem. Soc. 122, 1974-1978.    [Abstract]   [PDF]
  7. Torrents E, Buist G, Liu A, Eliasson R, Gibert I, Gräslund A, and Reichard P (2000) The anaerobic ribonucleotide reductase from Lactococcus lactis - catalytic properties and allosteric regulation of the pure enzyme system. J. Biol. Chem. 275, 2463-2471.    [Abstract]   [PDF]
  8. Davydov A, Liu A, and Gräslund A (2000) EPR evidence of two structurally different ferric sites in Mycobacterium tuberculosis ribonucleotide reductase R2-2 protein. J. Inorg. Biochem. 80, 213-218.    [Abstract]   [PDF]
  9. Liu A, Ho RYN, Que L Jr, Ryle MJ, and Hausinger RP (2001) Alternative reactivity of an α-ketoglutarate-dependent Fe(II) oxygenase: enzyme self-hydroxylation. J. Am. Chem. Soc. 123(21), 5126-5127.    [Abstract]   [PDF]
  10. Ho RYN, Mehn MP, Hegg EL, Liu A, Ryle MJ, Hausinger RP, and Que L Jr (2001) Resonance Raman studies of the Fe(II)-α-keto acid chromophore. J. Am. Chem. Soc. 123(21), 5022-5029.    [Abstract]   [PDF]
  11. Davydov A, Öhrström M, Liu A, and Gräslund A (2002) Chemical reduction of the diferric-radical center in protein R2 from mouse ribonucleotide reductase is independent of the proposed radical transfer pathway. Inorg. Chim. Acta 331, 65-72.    [Abstract]   [PDF]
  12. Liu A, Leese DN, Swarts JC, and Sykes AG (2002) Reduction of Escherichia coli ribonucleotide reductase with ferrocene derivatives. Inorg. Chim. Acta 337, 83-90.    [Abstract]   [PDF]
  13. Wang Y, Graichen ME, Liu A, Pearson AR, Wilmot CM, and Davidson VL (2003) MauG, a novel di-heme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry 42(24), 7318-7325.    [Abstract]    [PDF]
  14. Ryle MJ, Liu A, Muthukumaran RB, Koehntop KD, McCracken J, Que L Jr., and Hausinger RP (2003) O2- and α-ketoglutarate-dependent tyrosyl radical formation in TauD, an α-keto acid-dependent non-heme iron dioxygenase. Biochemistry 42(7), 1854-1862.    [Abstract]    [PDF]
  15. Jones LH, Liu A, Davidson VL (2003) An engineered CuA amicyanin capable of intramolecular electron transfer reactions. J. Biol. Chem. 278(47), 47269-47274.    [Abstract]    [PDF]
  16. Liu P, Liu A, Yan F, Wolfe MD, Lipscomb JD, and Liu HW (2003) Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme. Biochemistry 42(40), 11577-11586.    [Abstract]    [PDF]
  17. Ryle MJ, Koehntop KD, Liu A, Que L Jr, and Hausinger RP (2003) Interconversion of two oxidized forms of taurine/α-ketoglutarate dioxygenase, a nonheme iron hydroxylase: Evidence for bicarbonate binding.  Proc. Natl. Acad. Sci. U.S.A. 100(7), 3790-3795.   [Abstract]     [PDF]
  18. Zhou T, Mo Y, Liu A, and Tsai KR (2004) Enzymatic mechanism of Fe-only hydrogenase: density functional study on H-H making/breaking at the diiron cluster with concerted proton and electron transfers. Inorg. Chem. 43(3), 923-930.   [Abstract]    [PDF]
  19. Li T, Walker AL, Iwaki H, Hasegawa Y, Liu A (2005) Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor.  J. Am. Chem. Soc. 127(35), 12282-12290.    [Abstract]   [PDF]
  20. Liu A, Jin Y, Zhang J, Brazeau BJ, Lipscomb JD (2005) Substrate radical intermediates in soluble methane monooxygenase. Biochem. Biophys. Res. Commun. 338(1), 254-261.  (invited research article)     [Abstract]    [PDF]
  21. Colabroy KL, Zhai H, Li T, Ge Y, Zhang Y, Liu A, Ealick SE, McLafferty FW, and Begley TP (2005) The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3-hydroxyanthranilate. Biochemistry 44(21), 7623-7631.    [Abstract]    [PDF]
  22. Yan F, Li T, Lipscomb JD, Liu A, and Liu H-w (2005) Site-directed mutagenesis and spectroscopic studies of the iron-binding site of (S)-2-hydroxypropylphosphonic acid epoxidase. Arch. Biochem. Biophys. 442(1), 82-91.    [Abstract]   [PDF]
  23. Li T, Iwaki H, Fu R, Hasegawa Y, Zhang H, and Liu A (2006) α-Amino-β-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily. Biochemistry 45(21), 6628-6634.    [Abstract]    [PDF]
  24. Martynowski D, Eyobo Y, Li T, Yang K, Liu A, and Zhang H (2006) Crystallographic analysis of α-Amino-β-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD): Insight into the active site and catalytic mechanism of a novel decarboxylation reaction. Biochemistry 45(35), 10412-10421.   [Abstract]   [PDF]
  25. Liu A and Zhang H (2006) Transition metal-catalyzed nonoxidative decarboxylation reactions. Biochemistry (New Concepts), 45(35), 10407-10411. (This paper is being listed as a 2006 Hot Article on the ACS publications web site.)     [Abstract]    [PDF]
  26. Li T, Ma J, Hosler JP, Davidson VL and Liu A (2007) Detection of transient intermediates in the metal-dependent non-oxidative decarboxylation catalyzed by α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase.  J. Am. Chem. Soc. 129(30), 9278-9279.    [Abstract]     [PDF]
  27. Yan F, Moon S-J, Liu P, Zhao Z, Lipscomb JD, Liu A, and Liu H-w (2007) Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues. Biochemistry 46(44), 12628-12638.    [Abstract]     [PDF]
  28. Liu A, Li T, and Fu R (2007) Amidohydrolase Superfamily. In: Encyclopedia of Life Sciences. John Wiley & Sons, Ltd: Chichester http://www.els.net/ [DOI: 10.1002/9780470015902.a0020546]  (invited review article).    [Abstract]    [PDF]
  29. Li X, Fu R, Liu A, and Davidson VL (2008) Kinetic and physical evidence that the di-heme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone. Biochemistry 47(9), 2908-2912.    [Abstract]     [PDF]
  30. Munos JW, Moon S-J, Mansoorabadi SO, Hong L, Yan F, Liu A, and Liu H-w (2008) Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae. Biochemistry 47(33), 8726-8735. [Abstract]     [PDF]
  31. Li X, Fu R, Lee S, Krebs C, Davidson VL, and Liu A (2008) A catalytic di-heme bis-Fe(IV) form of MauG, Alternative to an Fe(IV)=O porphyrin radical. Proc. Natl. Acad. Sci. U.S.A. 105(25), 8597-8600.    [Abstract]     [PDF]
  32. Liu A (2009) EPR in Enzymology. In: Wiley Encyclopedia of Chemical Biology, John Wiley & Sons, Inc. (invited article), 1, 591-601      [Abstract]
  33. Huang Y, Zhou Y, Wong HC, Chen Y, Wang S, Castiblanco A, Liu A, Yang JJ (2009) A single EF-hand isolated from STIM1 forms dimer in the absence and presence of Ca2+, FEBS J. 276(19), 5589-5597.     [Abstract]     [PDF]
  34. Choi M, Sukumar N, Liu A, and Davidson VL (2009) Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine, Biochemistry 48(39), 9174-9184.     [Abstract]     [PDF]
  35. Fu R, Liu F, Davidson VL, Liu A (2009) Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands. Biochemistry (Rapid Report), in press.     [Abstract]    [PDF]

 

Courses Taught at Georgia State University (since 2008):

  1. Biochemistry I (CHEM 4600/6600), Fall 2008 (50%), 5 credit hours
  2. Biochemistry II (CHEM 6610), Spring 2009 (50%), 3.0 credit hours
  3. Biochemistry I (CHEM 4600/6600), Fall 2009 (100%), 5 credit hours
  4. Metals in Biology & Medicine (CHEM 4230/6230), Spring 2010 , 5 credit hours