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Biochemistry Faculty

Michael K. Chan


Dr. Chan
Professor and Interim Department Chair
(joint appointment with the Department of Chemistry)

Phone:  614-292-8375
Fax:      614-292-6773
email:  chan@chemistsry.ohio-state.edu
Webpage: Chan Homepage


Research Interests:

 The research of my laboratory is directed towards the study of metal based catalysts and sensors. These are interdisciplinary areas that require the use a wide variety of techniques from both chemical and biochemical disciplines.

 The focus of the biochemistry group is directed towards understanding the molecular mechanisms of metalloenzymes. Utilizing macromolecular crystallography, we obtain three-dimensional pictures of metalloproteins, and based on these structures, we form hypotheses for how they work.  My group is actively involved in several crystallographic studies, including peptide deformylase, a potential target for antibacterial chemotherapy; FixL, a heme based biological oxygen sensor; and Ni-CODH, an unusual biological enzyme capable of fundamental transformations of carbon monoxide.

 The research of the chemistry group emphasizes the design of functional synthetic systems which parallel the interests of the biological group. Here, projects involve the design and synthesis of new ligands, preparation of their associated metal complexes, and characterization of their physical and chemical properties. Current targets within the group are directed towards the design of heme analogs for asymmetric catalysis and chemical sensors.



Selected publications from the last 5 years:

Chan SI, Wang VC, Lai JC, Yu SS, Chen PP, Chen KH, Chen CL, Chan, M. K. (2007) "Redox Potentiometry Studies of Particulate Methane Monooxygenase: Support for a Trinuclear Copper Cluster Active Site." Angew Chem Int Ed Engl. 46(12), 1992-1994.

Isaza CE, Silaghi-Dumitrescu R, Iyer RB, Kurtz DM Jr, Chan, M. K. (2006) "Structural basis for O2 sensing by the hemerythrin-like domain of a bacterial chemotaxis protein: substrate tunnel and fluxional N terminus." Biochemistry. 45(30), 9023-31.

Jain R, Hao B, Liu RP, Chan, M. K.  (2006) "Structures of E. coli peptide deformylase bound to formate: insight into the preference for Fe2+ over Zn2+ as the active site metal.", J Am Chem Soc. 127(13), 4558-9.

Hao B, Zhao G, Kang PT, Soares JA, Ferguson TK, Gallucci J, Krzycki JA, Chan, M. K.  (2004) " Reactivity and chemical synthesis of L-pyrrolysine- the 22(nd) genetically encoded amino acid." Chem Biol. 11(9), 1317-24.

Blight SK, Larue RC, Mahapatra A, Longstaff DG, Chang E, Zhao G, Kang PT, Green-Church KB, Chan, M. K, Krzycki JA. (2004) " Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo." Nature 431(7006), 333-5.

Fekner T, Gallucci J, Chan, M. K.  (2004) "Synthesis and metalation of a chiral, pyridine-strapped, cyclic bis(benzimidazole) ligand.", Org Lett. 6(6), 989-92.

Fekner T, Gallucci J, Chan, M. K.  (2004) "Ruffling-induced chirality: synthesis, metalation, and optical resolution of highly nonplanar, cyclic, benzimidazole-based ligands." J Am Chem Soc.126(1), 223-36.

Fekner T, Gallucci J, Chan, M. K.  (2003) "Intramolecular aromatic nucleophilic substitution of the benzimidazole-activated nitro group.", Org Lett. 5(25), 4795-8.

Jain, R. and Chan, M. K. (2003) “Mechanisms of ligand discrimination by heme proteins”, J. Bioinorg. Chem. 8, 1-11.

Arndt, J.W., Hao, B., Ramakrishnan, V., Chen, T., Chan, S. I., and Chan, M. K. (2002) “Structure of the hyperthermophilic Pyrococcus furiosus carboxypeptidase”, Structure 10, 215-224.

Hao, B., Isaza, C., Arndt, J., Soltis, M., and Chan, M. K. (2002). "Structural analysis of the mechanism of oxygen sensing by the FixL heme domain of Bradyrhizobium japonicum", Biochemistry 41, 12952-12958.

Hao, B., Gong, W., Ferguson, T.K., James, C.M., Krzycki, J.A., and Chan, M. K. (2002) “Identification of novel UAG encoded residue: structure of a methanogen methyltransferase”, Science 296, 1462-1466.

Payra, P., S.C. Hung, W.H. Kwok, D. Johnston, J. Gallucci, Chan, M. K (2001).  "Structural Magnetic and Catalytic Properties of a Self-Recognized – Oxo-Bridged Diiron (III) Bis (benzimidazole) Complex”, Inorg. Chem. 40, 4036-4039.

Arndt, J.W., W. Gong, X. Zhong, J Liu, Z. Lin, A.K. Schowalter, C. Paxson, M.D. Tsai, Chan, M. K (2001).   “Insight into the Catalytic Mechanism of DNA Polymerase B: Structures of Intermediate Complexes”, Biochemistry 40, 5368-5375.

Chan, M. K. “Recent advances in heme-protein biosensors” (2001).  Curr. Opin Chem. Biol. 5, 216-222.

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The Ohio State University - Department of Biochemistry
776 Biological Sciences Building, 484 West 12th Avenue
Columbus, Ohio 43210
TEL: 614.292.6771
FAX: 614.292.6773
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