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Welcome to Feradical's Metalloprotein Research Laboratory 

Dr. Aimin Liu (a.k.a.: Feradical), Lutcher Brown Distinguished Professor in Biochemistry  

                      ORCID        ResearchGate    Google Scholar




Research in our lab studies how biomolecules utilize metals to perform the chemistry necessary for life. Specifically, we study mechanisms of oxygen activation by metalloenzymes and metalloproteins-mediated signal transduction regulation. To explore these phenomena, we utilize a wide array of techniques such as EPR spectroscopy, stopped-flow rapid kinetics, and protein X-ray crystallography. Our on-going research projects lie at the interface of chemistry and biology and span a broad range of topics including mechanistic enzymology, cofactor biogenesis, radical enzymology, natural product biosynthesis, and metalloprotein-mediated redox stress-linked transcriptional activation and gene regulation mechanisms.




2017     NSF Proposal Review Panelist

2017     Discussion Leader, Gordon Research Conference – Enzymes, Coenzymes, Metabolic Pathways, Waterville Valley, NH

2017     Panelist, Special Emphasis Panel, Center for Scientific Review, NIH

2017     253rd ACS National Meeting - Biochemistry - Symposium Chair: Metalloprotein-Initiated Signaling Transduction Response to Redox Stress, San Francisco, CA

2016-    Lutcher Brown Distinguished Chair in Chemistry, University of Texas at San Antonio

2016     Discussion Leader, Gordon Research Conference - Metals in Biology, Ventura, CA

2016     Panelist, Special Emphasis Panel, Center for Scientific Review, NIH

2015-6  Distinguished University Professor, Georgia State University (voluntarily relinquished in 01/2016 due to relocation to UTSA and appointed to Adjunct Professor)

2015-7  Alternate Councilor, American Chemical Society (ACS) Division of Biological Chemistry

2015     NSF Proposal Review Advisory Panelist

2015     Elected Member, Triennial Evaluation Committee of College of Arts & Sciences Dean, GSU

2015     Discussion Leader, GRC - Metals in Biology, Ventura, CA

2014     Outstanding Senior Faculty Award, College of Arts and Sciences, GSU

2014     Special Panelist, Speical Emphasis Panel, Center for Scientific Review, NIH

2014-    Faculty Senator, Georgia State University Senate

2013-    College Promotion & Tenure Committee – Natural and Computational Sciences (elected at-large seat)

2013-    International Expert - BBSRC & MRC, UK

2012     NSF Proposal Review Panelist

2012     Discussion Leader, GRC - Protein Cofactors, Radicals & Quinones, South Hadley, MA

2011     Chair, 40th Southeastern Magnetic Resonance Conference (SEMRC 2011)

2010-2  EMR Advisory Committee, The National High Magnetic Field Laboratory

2010-3  Director of Chemistry Core Facility, Natural Science Center, GSU

2009     NSF Proposal Review Panelist

2010     Session Chair, The Inaugural Annual Southeast Enzyme Conference

2009     Georgia Research Alliance Distinguished Cancer Scholar

2009     Cleon F. Arrington Research Initiation Award, Georgia State University

2008     Visiting Professor at Kansai University, Osaka, Japan

2006-8  Steering Committee Member, Neuroscience Graduate Curriculum, UMMC

2006     Macromolecular Structure and Function A (MSFA) Study Section, Center for Scientific Review, NIH

2005     Young Investigator Travel Award, National Ataxia Foundation

2003     Ralph E. Powe Junior Faculty Enhancement Award in Life Sciences, The Oak Ridge Associated
            Universities (ORAU)

2002     Paul D. Boyer Award for Research Excellence, University of Minnesota, MN

2002     Cyrus P. and Anne R. Barnum Travel Award, Minnesota Medical Foundation, Minneapolis, MN

2002     Young Investigator Award, The Seventh International Symposium of Spin Trapping

1998-9  Recipient, Wenner-Gren Foundation Fellowship, Stockholm, Sweden

1997     Poster 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
            (Silver medal shared with four colleagues), Beijing, China

1991     Presidential Award for Graduate Research, Chinese Academy of Sciences (CAS), Beijing, China



2013-    Editorial Board Member, BBA Proteins and Proteomics

2014-    Editorial Advisory Board, Journal of Biological Inorganic Chemistry (JBIC)

2016-9  Editorial Board Member, Reactive Oxygen Species (ROS)

2017-    Editorial Board Member, Frontiers in Bioscience

2017-    Editorial Board Member, Journal of Biochemistry and Chemical Sciences




  Probing ligand exchange in the P450 enzyme CYP121 from Mycobacterium tuberculosis: Dynamic equilibrium of the distal heme ligand as a function of pH and temperature
Fielding AJ, Fielding K, Ma L, Davis I, and Liu A
J. Am. Chem. Chem., 2017, 139(48), 17484-17499 [DOI]: 10.1021/jacs.7b08911   [PDF]

  Crosslinking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 from Mycobacterium tuberculosis proceeds through a catalytic shunt pathway
Dornevil K, Davis I, Fielding AJ, Terrell JR, Ma L, and Liu A
J. Biol. Chem., 2017, 292(33), 13645-13657 [DOI]: 10.1074/jbc.M117.794099   [PDF]

@    Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency
Ferreira F, Shin I, Sosova I, Dornevil K, Jain Shailly, Dewey D, Liu F, and Liu A
Molecular Genetics and Metabolism, 2017, 120(4), 317-324.

   A pitcher-and-catcher mechanism drives endogenous substrate isomerization by a dehydrogenase in kynurenine metabolism
Yang Y, Davis I, Ha U, Wang Y, Shin I, and Liu A
J. Biol. Chem., 2016, 291(51), 26252-26261 [DOI]: 10.1074/jbc.M116.759712
(designated by the editors as a "Papers of the Week" and selected, after publication, in a collection of a representative snapshot of recent papers in the field of Enzymology in a virtual issue)

@    An iron reservoir to the catalytic metal: The rubredoxin iron in an extradiol dioxygenase
Liu F, Geng J, Gumpper RH, Barman A, Davis I, Ozarowski A, Hamelberg D, and Liu A
J. Biol. Chem., 2015, 290(25), 15621-15634   [PDF]

@    Probing bis-Fe(IV) MauG: Experimental evidence for the long-range charge-resonance model
Geng J, Davis I, and Liu A
Angew. Chem. Int. Ed., 2015, 54, 3692-3696. DOI: 10.1002/anie.201410247   [PDF]

@    Crystallographic and spectroscopic snapshots reveal a dehydrogenase in action
Huo L, Davis I, Liu F, Andi B, Esaki S, Hiroaki I, Li T, Hasegawa Y, Orville AM, and Liu A
Nature Communications, 2015, 6:5935 [PDF]

@    Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): A structural and mechanistic unveiling
Huo L, Liu F, Hiroaki I, Hasegawa Y, and Liu A
PROTEINS, 2014, 83(1), 178-187 [PDF]

@    Pirin is an iron-dependent redox regulator of NF-κB     (F1000Prime Recommended Article)
Liu F, Rehmani I, Esaki S, Fu R, Chen L, Serroano V, and Liu A
Proc. Natl. Acad. Sci. U.S.A., 2013, 110(24), 9722-9727 (PNAS Direct Submission)    [PDF]

@   Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG
J, Dornevil K, Davidson VL, and Liu A
Proc. Natl. Acad. Sci. U.S.A., 2013, 110(24), 9639-9644 (PNAS Direct Submission)     [PDF]

@   Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis     (F1000Prime Recommended Article)
ET, Liu F, Krzystek J, Shin S, Jensen LMR, Davidson VL, Wilmot CM, and Liu A
Proc. Natl. Acad. Sci. U.S.A., 2013, 110(12), 4569-4573 (PNAS Direct Submission)    [PDF]

@    The power of two: arginine 51 and arginine 239* from a neighboring subunit are essential for catalysis in ACMS decarboxylase
L, Davis I, Chen L, and Liu A
J. Biol. Chem., 2013, 288(43), 30862-30871     [DOI]

@    Chemical rescue of the distal histidine mutants of tryptophan 2,3-dioxygenase
J, Dornevil K, and Liu A
J. Am. Chem. Soc., 2012, 134(29), 12209-12218     [DOI]

@   Evidence for a dual role of an active site histidine in α-amino-β-carboxymuconic-ε-semialdehyde decarboxylase
L, Fielding AJ, Chen Y, Li T, Iwaki H, Hosler JP, Chen L, Hasegawa Y, Que Jr, L, and Liu A
Biochemistry, 2012, 51(29), 5811-5821     [DOI]

@   The role of calcium in metalloenzyme: Effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG
Chen Y, Naik SG, Krzystek J, Shin S, Nelson WH, Xue S, Yang JJ, Davidson VL, and Liu A
Biochemistry, 2012, 51(8), 1586-1597     [DOI]

@   Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenase
Fu R, Gupta R, Geng J, Dornevil K, Wang S, Zhang Y, Hendrich MP, and Liu A
J. Biol. Chem., 2011, 286(30), 26541-26554     [PDF]

@    Mutagenesis of tryptophan199 suggests that electron hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis
Tarboush NA, Jensen LMR, Yukl ET, Geng J, Liu A, Wilmot CM, and Davidson VL
Proc. Natl. Acad. Sci. U.S.A., 2011, 108(41), 16956-16961     [PDF]

@   Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands
Fu R, Liu F, Davidson VL, and Liu A
Biochemistry, 2009, 48(49), 11603-11605     [DOI]

@   A catalytic di-heme bis-Fe(IV) form of MauG, alternative to an Fe(IV)=O porphyrin radical
Li X, Fu R, Lee S, Krebs C, Davidson VL, and Liu A
Proc. Natl. Acad. Sci. U.S.A., 2008, 105(25), 8597-8600 (PNAS Direct Submission)     [PDF]

@   Detection of transient intermediates in the metal-dependent nonoxidative decarboxylation catalyzed by α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase
Li T, Ma J, Hosler JP, Davidson VL and Liu A
J. Am. Chem. Soc., 2007, 129(30), 9278-9279     [DOI]

@   Transition metal-catalyzed nonoxidative decarboxylation reactions    (New Concepts Article)
Liu A and Zhang H
Biochemistry, 2006, 45(35), 10407-10411    [DOI]

@   α-Amino-β-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily
Li T, Iwaki H, Fu R, Hasegawa Y, Zhang H, and Liu A
Biochemistry, 2006, 45(21), 6628-6634     [DOI]

@    Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor
Li T, Walker AL, Iwaki H, Hasegawa Y, and Liu A
J. Am. Chem. Soc., 2005, 127(35), 12282-12290     [DOI]





NIGMS/NIH; NIMH/NIH; NSF; and Lutcher Brown Distinguished Chair Endowment.