CV of Dr.

Guohua Zhao

Curricula Vitae
Personal information:
Name: Guohua Zhao, Ph.D. of Biochemistry
Address: 5 Turn About Lane, Sicklerville, NJ 08081.
Home Phone: 1-856-629-3605, Cell Phone: 1-215-873-5811.
E-mail: gzhao2@comcast.net
Civil Status: Citizen of USA

Summary
More than 12 years research experiences (with 7 years Sr. Research Assistant experience)
in the fields of Molecular Biology, Biochemistry, Enzymology and Protein Science.
Main experiences are focused on the Enzyme’s structure and function studies, drug
discovery through kinetics studies, protein mutagenesis, the amino acid residue function
exploration and the new inhibitors designation and finding, with the publication on the peer
academic journals.
The main experiences also include: Cell culture, High throughput Screening (HTS), gene
cloning, DNA re-combination, protein expression and purification, enzyme/protein modification
and characterization, plasmid library and primer designation, and E. coli gene knock out, data
analyzing and trouble-shooting. The experience for lab administration and being a supervisor to
direct junior scientists are plus.
The experience for the protein crystallization is a plus
The modern related bench-top techniques also include immuno-detection methods such as
ELISA, Northern block. The instrumental assay techniques such as Spectrophotometer,
fluorescence photometer, Circular Dichroism photometer, HPLC, FPLC, Stopped Flow system,
and LC-LC/MS and so on.
Familiar the Microsoft Office tools.

Employment History and Work Experiences

Sr. Research Assistant (11/2002 – Present)

Department of Biochemistry, Drexel University, College of Medicine.
With the sarcosine oxidase as research material, the main work is focused on the enzyme’s
structure and function. Through mutagenesis, kinetics, inhibition, function of specific amino acid
residue stusies to find out potential drug. The researchs are related in the fields of Molecular
Biology, Biochemistry, Protein Science and Enzymology

Post-Doctoral fellow (1/1999 – 11/2002)

Department of Biochemistry, Drexel University, College of Medicine.
The work is focused on the mechanism of flavo-containing oxidase by comparing the wild type
enzyme and its mutants to interact with the substrate and bind with the substrate analog inhibitors.

Post-Doctoral fellow (10/1996 - 12/1998)

Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma.
The work is focused on solving the crystal structure of Staphylokinase, which is an important
enzyme in resolving the blood clot (thrombus) formed in blood vessel and is a kind of clinic
pharmacy for treat the heart disease and the stroke

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 CV of Dr. Guohua Zhao

Education

09/1990 - 06/1996 Ph.D. of Biochemistry

Protein Engineering Center & Laboratory of Enzymology,
Department of Chemistry
University of Liège, Liège, Belgium
Thesis: The mechanism of DD-peptidase, a penicillin sensitive peptidase.
Degree: 1996.

Publications

1. Guohua Zhao, Robert C. Brunckner and Marilyn Schuman Jorns (2008), Identification of
the Oxygen Activation Site in Monomeric Sarcosine Oxidase: Role of Lys265 in Catalysis.
Biochemistry, 47(35): 9124 – 9135.
2. Guohua Zhao and Marilyn Schumann Jorns (2006), Spectral and kinetic characterization of
the michaelis charge transfer complex in monomeric sarcosine oxidase. Biochemistry,
45(19): 5985 – 5992.
3. Guohua Zhao and Marilyn Schumann Jorns (2005), Ionization of Zwitterionic Amine
Substrates Bound to Monomeric Sarcosine Oxidase. Biochemistry, 44(51): 16866 – 16874.
4. Guohua Zhao, Hui Song, Zhi-wei Chen, F. Scott and Marilyn S. Jorns (2002). Monomeric
Sarcosine Oxidase: Role of Histidine 269 in Catalysis. Biochemistry, 41(31): 9751 - 9764.
5. Guohua Zhao and Marilyn Schumann Jorns (2002), Monomeric Sarcosine Oxidase:
Evidence for an Ionizable Group in the E•S Complex. Biochemistry, 41(31): 9747 - 9750.
6. Guohua Zhao, Qu J., Davis FA and Marilyn Jorns (2000), Inactivation of Monomeric
Sarcosine Oxidase by Reaction with N-(Cyclopropyl)glycine, Biochemistry, 39: 14341-
14347.
7. Zhao, G. H. et al and Frère, J. M. (1997), Site-Directed Mutagenesis of Actinomadura R39
DD-Peptidase, Biochem. J., 327(2): 377-381.
8. Zhao, G. H. and Frère, J. M. (1997), Reversible Inhibition of Enzymatic Systems Involving
Covalent Intermediates, J. Enzym. Inhib., 11(4): 245-264.
9. Wilkin et al, Zhao, G. H. et al (1993), The Mechanism of Action of DD-Peptidase: The Role
of Tyrosine-159 in the Streptomyces R61 DD-Peptidase, Biochem. J., 291: 537 - 544.
10. Damblon C, Zhao, G. H. et al (1995), Breakdown of the Stereospecificity of DD-Peptidases
and β-Lactamases with Thiolester Substrates, Biochem. J., 309: 431-436.
11. David Venci, Guohua Zhao and Marilyn S. Jorns (2002), Molecular Characterization of
NikD, a New Flavoenzyme Important in the Biosynthesis of Nikkomycin Antibiotics,
Biochemistry, 41(52): 15795 - 15802.
12. Bruckner, R.C., Zhao, G., Venci, D. and Jorns, M.S.(2004), Nikkomycin biosynthesis:
formation of a 4-electron oxidation product during turnover of NikD with its physiological
substrate, Biochemistry, 43(28), 9160 – 9167.
13. Hassan-Abdallah A, Bruckner RC, Zhao G, Jorns MS (2005), Biosynthesis of covalently
bound flavin: isolation and in vitro flavinylation of the monomeric sarcosine oxidase
apoprotein, Biochemistry. 44(17):6452-62.
14. Hassan-Abdallah A, Zhao G, Eschenbrenner M, Chen ZW, Mathews FS, Jorns MS, (2005),
Cloning, expression and crystallization of heterotetrameric sarcosine oxidase from
Pseudomonas maltophilia, Protein Expression and Purification, 43(1):33-43.

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 CV of Dr. Guohua Zhao

15. Chen ZW, Zhao G, Martinovic S., Jorns MS and Mathews FS (2005), Structure of the
sodium borohydride-reduced N-(cyclopropyl)glycine adduct of the flavoenzyme monomeric
sarcosine oxidase, Biochemistry, 44(47): 15444 – 15450.
16. Chen ZW, Hassan-Abdallah A, Zhao G, Jorns MS and Mathews FS (2006), Heterotetrameric
Sarcosine Oxidase: Structrue of a Diflavin Metalloenzyme at 1.85A Resolution, J. Mol. Biol.,
360(5): 1000 – 1018.
17. Mathews, FS, Chen, ZW, Trickey, P, Hassan-Abdullah, A, Zhao, G and Jorns, MS (2005).
Structure at 1.85A Resolution of Heterotetrameric Sarcosine Oxidase. The 15th International
Symposium on Flavins and Flavoproteins, pp 93 - 104, April 17 – 22, Shonan Village Center,
Hayama, Japan. Edit Nishino, T, Miura, R, Tanokura, M and Fukui, K. ArchiTect inc. Japan.
18. Jorns, MS, Hassan-Abdallah, A, Bruckner, RC and Zhao, G. (2005), Autocatalytic
Flavinylation of Monomeric Sarcosine Oxidase Apoprotein. The 15th International
Symposium on Flavins and Flavoproteins, pp 675 - 680, April 17 – 22, Shonan Village Center,
Hayama, Japan. Edit Nishino, T, Miura, R, Tanokura, M and Fukui, K. ArchiTect inc. Japan.
19. Jorns MS, Bruckner RC, Zhao G., Carrell CJ and Mathews FS (2005), NikD: Crystal
Structure, Charge Transfer Complex and Endogenous Ligands, The 15th International
Symposium on Flavins and Flavoproteins, pp 773 - 785, April 17 – 22, Shonan Village Center,
Hayama, Japan. Edit Nishino, T, Miura, R, Tanokura, M and Fukui, K. ArchiTect inc. Japan.
20. Hassan-Abdallah, A, Zhao, G and Jorns, MS (2006). Role of the Covalent Flavin Linkage in
Monomeric Sarcosine Oxidase. Biochemistry, 45(31), 9454 – 9462.
21. Bruckner RC, Zhao, G, Ferreira P and Jorns MS (2007). A mobile tryptophan is the intrinsic
charge transfer donor in a flavoenzyme essential for nikkomycin antibiotic biosynthesis.
Biochemistry, 46(3), 819 – 827.
22. Carrell, CJ, Bruckner, RC, Venci, D, Zhao, G., Jorns, MS and Mathews, FS (2007). NikD,
an Unusual Amino Acid Oxidase Essential for Nikkomycin Biosynthesis: Structures of
Closed and Open Forms at 1.15 and 1.90 Å Resolution, Structure, 15(8), 928 – 941.
23. Hassan-Abdallah, A, Zhao, G and Jorns, MS (2008). Covalent Flavinylation of Monomeric
Sarcosine Oxidase: Identification of a Residue Essential for Holoenzyme Biosynthesis.
Biochemistry, 47(4), 1136 – 1143.
24. Hassan-Abdallah, A, Zhao, G, Chen, ZW, Mathews, FS and Jorns, MS (2008). Arginine R49
Is a Bifunctional ResidueInportant in Catalysis and Biothynthesis of Monomeric Sarcosine
Oxidase: A Context Sensitive Model for the Electrostadic Impact of Arginine to Lysine
Mutation. Biochemistry, 47(9), 2913 – 2922.