Suganya Sumithran, Ph.D. - Publications
Affiliations: | University of South Carolina, Columbia, SC |
Area:
Bio-inorganic, bio-physical, and bio-organic chemistry; spectroscopy and mechanisms of action of dioxygen- and peroxide-activating heme iron enzymes and model systems; cytochrome P-450; magnetic circular dichroism spectroscopyYear | Citation | Score | |||
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2012 | Sumithran S, Sono M, Raner GM, Dawson JH. Single turnover studies of oxidative halophenol dehalogenation by horseradish peroxidase reveal a mechanism involving two consecutive one electron steps: toward a functional halophenol bioremediation catalyst. Journal of Inorganic Biochemistry. 117: 316-21. PMID 23102773 DOI: 10.1016/J.Jinorgbio.2012.09.017 | 0.461 | |||
2009 | Droghetti E, Sumithran S, Sono M, Antalík M, Fedurco M, Dawson JH, Smulevich G. Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH. Archives of Biochemistry and Biophysics. 489: 68-75. PMID 19622342 DOI: 10.1016/J.Abb.2009.07.008 | 0.503 | |||
2008 | Sook BR, Block DR, Sumithran S, Montañez GE, Rodgers KR, Dawson JH, Eichenbaum Z, Dixon DW. Characterization of SiaA, a streptococcal heme-binding protein associated with a heme ABC transport system. Biochemistry. 47: 2678-88. PMID 18247478 DOI: 10.1021/Bi701604Y | 0.58 | |||
2007 | Sumithran S, Dawson JH. Characterization of the heme binding properties of Staphylococcus aureus IsdA Chemtracts. 20: 69-77. | 0.467 | |||
2006 | Osborne RL, Sumithran S, Coggins MK, Chen YP, Lincoln DE, Dawson JH. Spectroscopic characterization of the ferric states of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase: His-ligated peroxidases with globin-like proximal and distal properties. Journal of Inorganic Biochemistry. 100: 1100-8. PMID 16603247 DOI: 10.1016/J.Jinorgbio.2006.02.008 | 0.51 | |||
2005 | Eakanunkul S, Lukat-Rodgers GS, Sumithran S, Ghosh A, Rodgers KR, Dawson JH, Wilks A. Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae. Biochemistry. 44: 13179-91. PMID 16185086 DOI: 10.1021/Bi050422R | 0.573 | |||
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