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Aimin Liu

                  Dr. Aimin Liu

                  Associate Professor
                  GCC Distinguished Scholar
                  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

 

Courses Taught at Georgia State (since Fall 2008)

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

Research Interest: 1) 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 Distinctions

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 Faculty Seminars & Talks in Scientific Meetings (since independent career)

12/2009   Emory University (Colloquium)
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 - Protein Cofactors, Radicals, and Quinones, Ventura, CA
 10/2007   Pennsylvania State University
 01/2006   Gordon Research Conferences - Metals in Biology, Ventura, CA
 01/2006   The Inaugural Texas Enzyme Mechanism Conference, Austin, TX
 11/2003   Poster talk, Gordon Research Conferences - Enzyme, Coenzyme & Metabolic Pathways
 06/2003   Jackson State University - NIH-Sponsored SCORE Seminar Series
 02/2003   Mississippi State University

Recent Peer-Reviewed Research Articles (past five years)

  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. Liu A (2009) EPR in Enzymology. In: Wiley Encyclopedia of Chemical Biology, John Wiley & Sons, Inc. (invited article), 1, 591-601.  [Abstract]
  15. 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]
  16. 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]
  17. 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), 48(49), 11603-11605.     [Abstract]    [PDF]
  18. Gupta R, Fu R, Liu A, and Hendrich M (2010) EPR and Mössbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase. J. Am. Chem. Soc., 132(3), 1098-1109.    [Abstract]    [PDF]