Feradical (Aimin) Liu, Ph.D.
Georgia State University
Atlanta, GA 30303-4098
Email: Feradical (at) gsu.edu


LIST OF PUBLICATIONS

I. Work Since Independent Research (up to February 2012)

58.    Decarboxylation mechanisms in biological system (Invited Review)

 Tingfeng Li, Lu Huo, Christopher Pulley, and Liu A

  Bioorg. Chem., 2012, xx, in press

57.    The role of calcium in metalloenzyme: Effects of calcium removal on the axial ligation geometry and magnatic 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, 1586-1597

56.    Tryptophan tryptophylquinone biosynthesis: A radical approach to posttranslational modification (Invited Review)

 Davidson VL and Liu A

  Biochim. Biophys. Acta , 2012, 1xx, in press

55.    Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG

 Feng M, Jensen LMR, Yukl ET, Wei X, Liu A, Wilmot CM, and Davidson VL

  Biochemistry , 2012, 51, 1598-1606

54.    The roles of Rhodobacter sphaeroides copper chaperones PCu_AC and Sco (PrrC) in the assembly of the copper centers of the aa₃-type and the cbb₃-type cytochrome c oxidases

 Thompson AK, Gray J, Liu A, Hosler JP

  Biochim. Biophys. Acta , 2012, 1817, 955-964

53.    Synthesis, characterisation, and preliminary in vitro studies of vanadium(IV) complexes with a schiff base and thiosemicarbazones as mixed ligands

 Lewis NA, Liu F, Seymour L, Magnusen A, Erves TR, Arca JF, Beckford FA, Venkatraman R, Gonz·lez-SarrÌas A, Fronczek FR, VanDerveer DG, Seeram NP, Liu A, Jarrett WJ, Holder AH

  Eur. J. Inorg. Chem., 2012, 4, 664-677

52.    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

51.    The reactivation mechanism of tryptophan 2,3-dioxygenase by hydrogen peroxide

 Fu R, Gupta R, Geng J, Dornevil K, Wang S, Hendrich MP, and Liu A

 J. Biol. Chem., 2011, 268, 26541-26554

 

50.  Nature's strategy for oxidizing tryptophan: EPR and Mössbauer characterization of the unusual high-valent heme iron intermediates. Book Chapter in: Mossbauer Spectroscopy:  Applications in Chemistry, Biology, Industry, and Nanotechnology. 

      Dornevil K and Liu A, edited by Virender K. Sharma, Goestar Klingelhoefer, and Tetsuaki Nishida, 2011, in press

 

49.  Redox and oxygen sensing in the regulation of transcription by metalloproteins. Book Chapter in: Molecular Basis of Oxidative Stress: Chemistry, Mechanisms and Disease Pathogenesis.

       Rehmani I, Liu, F and Liu A, edited by Frederick A. Villamena, John Wiley & Sons, Inc., 2011, in press

 

48.  The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis

Shin S, Feng M, Chen Y, Jensen LMR, Tachikawa H, Wilmot CM, Liu A, and Davidson VL

Biochemistry, 2011, 50, 144-150.

 

47.  Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface

Choi M, Sukumar N, Mathews FS, Liu A and Davidson VL

Biochemistry, 2011, 50, 1265-1273.

 

46.  EPR and Mössbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase

Gupta R, Fu R, Liu A, and Hendrich MP

J. Am. Chem. Soc. 2010, 132, 1098-1109.

 

45.  Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: Insights into the assembly of Cu_B of cytochrome c oxidase

Thompson, AK, Smith D, Gray J, Carr HS, Liu A, Winge DR, Hosler JP 

Biochemistry, 2010, 49, 5651-5661.

 

44.  Heme iron nitrosyl complex of MauG reveals efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands

Fu R, Liu F, Davidon VL, and Liu A

Biochemistry, 2009, 48, 11603-11605.

 

43.  Electron Paramagnetic Resonance (EPR) in Enzymology

       Liu A

       Wiley Encyclopedia of Chemical Biology, 2009, 1, 591-601, John Wiley & Sons, Inc.

 

42.  A single EF-hand isolated from STIM1 forms dimer in the absence and presence of Ca²⁺

Huang Y, Zhou Y, Wong HC, Chen Y, Wang S, Castiblanco A, Liu A, Yang JJ.

FEBS J. 2009, 276, 5589-5597.

 

41.  Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine

Choi M, Sukumar N, Liu A, and Davidson VL

Biochemistry, 2009, 48, 9174-9184.

 

40.  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, 8597-8600.

 

39.  Kinetic and physical evidence that the di-heme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone

Li X, Fu R, Liu A, and Davidson VL

Biochemistry, 2008, 47, 2908–2912.

 

 

38.  Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae

Munos JW, Moon S-J, Mansoorabadi SO, Hong L, Yan F, Liu A, and Liu H-w

      Biochemistry, 2008, 47, 8726–8735.

 

37.  Amidohydrolase Superfamily

Liu A, Li T, and Fu R

Encyclopedia of Life Sciences (September 2007), John Wiley & Sons, Ltd: Chichester http://www.els.net/ [DOI: 10.1002/9780470015902.a0020546] (Invited Review).

 

36.  Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropyl phosphonic acid epoxidase using ¹⁷O-enriched substrates and substrate analogues

Yan F, Moon S-J, Liu P, Zhao Z, Lipscomb JD, Liu A, and Liu H-w

Biochemistry, 2007, 46, 12628-12638.

 

35.  Detection of transient intermediates in the metal-dependent non-oxidative decarboxylation catalyzed by α-amino-b-carboxymuconate-ε-semialdehyde decarboxylase

Li T, Ma J, Hosler JP, Davidson VL, and Liu A

J. Am. Chem. Soc., 2007, 129, 9278-9279.

 

34.  α-Amino-b-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily

Li T, Iwaki H, Fu R, Hasegawa Y, Zhang H, Liu A

Biochemistry, 2006, 45, 6628-6634.

 

33.  Crystallographic analysis of α-amino-b-carboxymuconic-ε-semialdehyde decarboxylase: Insight into the active site and catalytic mechanism of a novel decarboxylation reaction

Martynowski D., Eyobo Y., Li T, Yang K., Liu A, and Zhang H

Biochemistry, 2006, 45, 10412-10421.

 

 

32.  Transition metal-catalyzed nonoxidative decarboxylation reactions

Liu A and Zhang H

Biochemistry, 2006, 45, 10407-10411.

 

31.  The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3 hydroxyanthranilate

Colabroy KL, Zhai H, Li T, Ge Y, Zhang Y, Liu A, Ealick SE, McLafferty FW, and Begley TP

Biochemistry, 2005, 44, 7623–7631.

 

30.  Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor

Li T, Walker AL, Iwaki H, Hasegawa Y, Liu A

J. Am. Chem. Soc., 2005, 127, 12282–12290.

 

29.  Site-directed mutagenesis and spectroscopic studies of the iron-binding site of (S)-2 hydroxypropylphosphonic acid epoxidase

Yan F, Li T, Lipscomb JD, Liu A, and Liu HW

Arch. Biochem. Biophys., 2005, 442, 82–91.

 

28.  An engineered Cu_A amicyanin capable of intramolecular electron transfer reactions

Jones LH, Liu A, and Davidson VL

J. Biol. Chem., 2003, 278, 47269–47274.

 

27.  MauG, a novel di-heme protein required for tryptophan tryptophylquinone biogenesis

Wang Y., Graichen ME, Liu A, Pearson AR, Wilmot CM, and Davidson VL

Biochemistry, 2003, 42, 7318–7325.

 

 

II.  Work from Postdoctoral Research

 

26.  Substrate radical intermediates in soluble methane monooxygenase

 Liu A, Jin Y, Zhanga J, Brazeaua BJ and Lipscomb JD.

 Biochem. Biophys. Res. Commun., 2005, 338, 254–261.

 

25.  O₂- and a-ketoglutarate-dependent tyrosyl radical formation in TauD, an a-keto acid dependent non-heme iron dioxygenase

        Ryle MJ, Liu A, Muthukumaran RB, Koehntop KD, McCracken J, Que L Jr., and Hausinger RP. Biochemistry, 2003, 42, 1854–1862.

 

24.  Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme

        Liu P, Liu A, Yan F, Wolfe MD, Lipscomb JD, and Liu HW

        Biochemistry, 2003, 42, 11577–11586.

 

23.  Interconversion of two oxidized forms of taurine/a-ketoglutarate dioxygenase, a nonheme iron hydroxylase: Evidence for bicarbonate binding

        Ryle MJ, Koehntop KD, Liu A, Que L Jr, and Hausinger RP

Proc. Natl. Acad. Sci. U. S. A., 2003, 100, 3790–3795.

 

22.  Reduction of Escherichia coli ribonucleotide reductase with ferrocene derivatives

        Liu A, Leese DN, Swarts JC, and Sykes AG

Inorg. Chim. Acta, 2002, 337, 83–90 (special edition, invited paper).

 

21.   Resonance Raman studies of the Fe(II)-a-keto acid chromophore

Ho RYN, Mehn MP, Hegg EL, Liu A, Ryle MJ, Hausinger RP, and Que L Jr

         J. Am. Chem. Soc., 2001, 123, 5022–5029.

 

20.   Alternative reactivity of an α-ketoglutarate-dependent Fe(II) oxygenase: enzyme self hydroxylation

Liu A, Ho RYN, Que L Jr, Ryle MJ, and Hausinger RP

         J. Am. Chem. Soc., 2001, 123, 5126–5127.

 

 

III.  Work from Graduate Research

 

19.   Chemical reduction of the diferric-radical center in protein R2 from mouse ribonucleotide reductase is independent of the proposed radical transfer pathway

         Davydov A, Öhrström M, Liu A, and Gräslund A

         Inorg. Chim. Acta, 2002, 331, 65–72.

 

18.  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

        Liu A and Gräslund A

        J. Biol. Chem., 2000, 275, 12367–12373.

 

17.  Yeast ribonucleotide reductase—a new type of ribonucleotide reductase with a heterodimeric iron-radical containing subunit

        Chabes A, Domkin V, Larsson G, Liu A, Gräslund A, Wijmenga S, and Thelander L

        Proc. Natl. Acad. Sci. U. S. A., 2000, 97, 2474–2479.

 

16.  Heterogeneity of the local electrostatic environment of the tyrosyl radical in Mycobacterium tuberculosis ribonucleotide reductase observed by high-field EPR spectroscopy

        Liu A, Barra AL, Rubin H, Lu G, and Gräslund A

        J. Am. Chem. Soc., 2000, 122, 1974–1978.

 

15. The anaerobic ribonucleotide reductase from Lactococcus lactis – catalytic properties and allosteric regulation of the pure enzyme system

       Torrents E, Buist G, Liu A, Eliasson R, Gibert I, Gräslund A, and Reichard P

       J. Biol. Chem., 2000, 275, 2463–2471.

 

14.  EPR evidence of two structurally different ferric sites in Mycobacterium tuberculosis ribonucleotide reductase R2-2 protein

        Davydov A, Liu A, and Gräslund A.

        J. Inorg. Biochem., 2000, 80, 213–218.

 

 

13.  Sequential mechanism of methane dehydrogenation over metal oxide and carbide catalysts

        Zhou T, Liu A, Mo Y, and Zhang H

        J. Phys. Chem. A, 2000, 104, 4505–4513.

 

12.  The interaction between iron and the protein radical in aerobic and anaerobic ribonucleotide reductases

        Liu A. Doctoral Thesis, Akademitryck AB 2000, Stockholm, Sweden, ISBN 91-7265-101-6, pp. 1-46.

 

11.  New paramagnetic species formed at the expense of the transient tyrosyl radical in mutant  protein R2 F208Y of Escherichia coli ribonucleotide reductase

        Liu A, Sahlin M, Pötsch S, Sjöberg BM, Gräslund A

        Biochem. Biophys. Res. Commun., 1998, 246, 740–745.

 

10.  The tyrosyl free radical of recombinant ribonucleotide reductase from Mycobacterium tuberculosis is located in a rigid hydrophobic pocket

        Liu A, Pötsch S, Davydov A, Barra A, Rubin H, and Gräslund A

        Biochemistry, 1998, 37, 16369–16377.

 

 

IV.  Work from China

 

9.  Enzymatic mechanism of Fe-only hydrogenase: density functional study on H-H making/breaking at the diiron cluster with concerted proton and electron transfers

      Zhou T, Mo Y, Liu A, and Tsai KR

      Inorg. Chem., 2004, 43, 923–930.

 

8.  Optimal group symmetric localized molecular orbitals

       Zhou T and Liu A.

      Theoret. Chim. Acta, 1994, 88, 375-381.

 

7.  Symmetry-adaptation of configuration basis in MCSCF method

     Zhou T and Liu A.

    Theoret. Chim. Acta, 1994, 89, 137-145.

 

6.  Study of localized molecular orbitals using group theory methods and its approach to the multi electron correlation problem: The symmetric reduction of multi-center integrals in multiconfigurational self-consistent-field approach

      Zhou T and Liu A

      J. Comp. Chem., 1994, 15, 858-865.

 

5.  Oxygenation of methane to methanol by methane monooxygenase of Methylomonas species GYJ-3

     Liu A and Li S

     J. Nat. Gas Chem., 1993, 2, 109–118.

 

4.  Formation of propylene oxide by Methylomonas GYJ-3 in a gas-solid bioreactor

     Li S, Gao C, and Liu A

     Chinese Chem. Lett., 1991, 4, 303–306.

 

3.  Stereoselectivity of styrene oxide from styrene epoxidation by Methylomonas sp. GYJ3

      Liu A, Li S, Miao D, Liu P, and Yu W

     Fenzi Cuihua (Molecular Catalysis, in Chinese), 1991, 5, 377–381.

 

2.  Isolation and purification of methane monooxygenase from Methylomonas species GYJ-3

     Liu A, Li S, Miao D, Yu W, Zhang F, and Su P

     Chinese Chem. Lett., 1991, 2, 419–422.

 

1. Preparative slab electrofocusing of methane monooxygenase from a type I methanotroph Methylomonas GYJ-3

     Liu A, Li S, Yu W, Zhang F, Chen J, and Su P

    Biochem. I., 1990, 22, 959-965.

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EPR spectroscopy is a pertinent tool for detecting and characterizing metals ions and free radicals.