Hiroyasu Tachikawa

Professor Emeritus

 tach_sz 1400 J. R. Lynch Street, P.O. Box 17910
Jackson, MS39217-0510

Physical location:
John A.Peoples Science Building
Office: room #508

Contact:
E-mail: hiroyasu.tachikawa@jsums.edu
Tel: (601) 979-3485
Fax: (601) 979-3674

Teaching

Advanced Analytical Chemistry
Special Topics is Analytical Chemistry
Electrochemical and Optical Sensors


Research Interests
:

Electrochemical biosensors.  Raman spectroscopy of thin films and biomolecules: Current research interests of our group are development of biosensors for biomedical import species and characterization of proteins using electrochemical methods and spectroscopies which include Raman, FT-IR, and UV-Vis. 


Selected publications (Click here for full list)

  1. Shin, S., Feng, M., Chen, Y., Jensen, L.M.R., Tachikawa, H., Wilmot, C.M., Liu, A., Davidson, V.L. The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis, Biochemistry 50 (1) , pp. 144-150, 2011.
  2. Abu Tarboush, N., Jensen, L.M.R., Feng, M., Tachikawa, H., Wilmot, C.M., Davidson, V.L. Functional importance of tyrosine 294 and the catalytic selectivity for the Bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine, Biochemistry 49 (45) , pp. 9783-9791, 2010.
  3. M. Feng and H. Tachikawa, Surface-Enhanced Resonance Raman Spectroscopic Characterization of the Protein Native Structure, J. Am. Chem. Soc.,130, 7443-7448 (2008).
  4. Zhang, M. Feng, and H. Tachikawa, Layer-by-layer Fabrication and Direct Electrochemistry of Glucose Oxidase on Single Wall Carbon Nanotubes, Biosens. Bioelectron., 22, 3036-3041 (2007).
  5. X. Li, M. Feng, Y. Wang, H. Tachikawa, and V.L. Davidson, Evidence for redox cooperativity  between c-type hemes of Mau-G which is likely coupled to oxygen activation during tryptopan tryptophyl quinine biosynthesis, Biochemistry45, 821-828 (2006).
  6. H. Han and H. Tachikawa, Electrochemical Determination of Thiols at Single-Wall Carbon Nanotubes and PQQ Modified Electrodes, Frontier in Bioscience, 10, 931-939 (2005).
  7. A. Ray, M. Feng, and H. Tachikawa, Direct electrochemistry and Raman spectroscopy of sol-gel-encapsulated myoglobin, Langmuir21, 7456-7460 (2005).
  8. M. Feng, H. Tachikawa, X. Wang, T.D. Pfister, A.J. Gengenbach, and Y. Lu, Resonance Raman Spectroscopy of Cytochrome c Peroxidase Variants, that Mimic Manganese Peroxidase, J. Biol. Inorg. Chem., 8, 699-706 (2003).
  9. L. Bao, D. Sun, H. Tachikawa, and V. L. Davidson, Improved Sensitivity of a Histamine  Sensor Using an Engineered Methylamine Dehydrogenase, Anal. Chem., 74, 1144-1148 (2002).
  10. M. Feng and H. Tachikawa, Raman Spectroscopic and Electrochemical Characterization of  Myoglobin Thin Film: Implication of the Role of Histidine 64 for Fast Heterogeneous Electron Transfer, J. Am. Chem. Soc., 123, 3013-3020 (2001).