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Address and Contact Information
- Dr Sci, Russian Academy of Sciences
- PhD, Russian Academy of Sciences
- Diploma, Novosibirsk State University, Russia
- Continuous-wave, time-domain and high-field Electron Paramagnetic Resonance
- Magnetic resonance as a structural tool in solid states and its applications in protein structure, inorganic biochemistry, photosynthesis, catalysis, radiation chemistry and medicine
- Bioenergetics and photosynthesis
- Iron-sulfur proteins
- Nitroxide radicals and spin labels
- Structure-function relations in metalloproteins
- Quinone processing sites
- Metals and metal-based drugs in medicine
- Martin E, Samoilova RI, Narasimhulu KV, Wraight CA, Dikanov SA. 2010. Hydrogen bonds between nitrogen donors and the semiquinone in the QB-site of bacterial reaction centers. J. Am. Chem. Soc. 132, 11671-11677.
- Yi SM, Naraimhul KV, Samoilova RI, Gennis KB, Dikanov SA. 2010. Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxi dase of Bacillus subtilis. J. Biol. Chem. 285, 18241-18251.
- Lhee S, Kolling DRJ, Nair SK, Dikanov SA, Crofts AR. 2010. Modifications of protein environment of the [2Fe-2S] cluster of the bc1 complex: Effects in the biophysical properties of the Rieske iron-sulfur protein and the kinetics of the complex. J. Biol. Chem. 285, 9233-9248.
- Iwasaki T, Samoilova RI, Kounosu A, Dikanov SA. 2009. Two-dimensional Pulsed Electron Spin Resonance Characterization of 15N-Labeled Archaeal Rieske-type Ferredoxin. FEBS Lett. 583, 3467-3472.
- Iwasaki T, Samoilova RI, Kounosu A, Ohmori D, Dikanov SA 2009. Continuous-wave and pulsed EPR characterization of the [2Fe-2S](Cys)3(His)1 cluster in rat MitoNEET. J. Am. Chem. Soc. 131, 13659-13667.
- Dikanov SA, Samoilova RI, Kappl R, Crofts AR, Hüttermann J. 2009. The reduced [2Fe-2S] clusters in adrenodoxin and Arthrospira platensis ferredoxin share spin density with protein nitrogens, probed using 2D ESEEM. Phys. Chem. Chem. Phys. 11, 6807 - 6819.
- Kolling DRJ, Samoilova RI, Shubin AA, Crofts AR, Dikanov SA. 2009. Proton environment of reduced Rieske iron-sulfur cluster probed by two-dimensional ESEEM spectroscopy J. Phys. Chem. A, 113 (4), 653-667.
- Lin MT, Samoilova RI, Gennis RB, Dikanov SA. 2008. Identification of the nitrogen donor hydrogen bonded with the semiquinone at the QH Site of the cytochrome bo3 from Escherichia coli. J. Am. Chem. Soc. 130, 15768-15769.
- Crofts AR, Holland JT, Victoria D, Kolling DRJ, Dikanov SA, Gilbreth R, Lhee S, Kuras R, Guergova-Kuras M. 2008. Is the modified Q-cycle sufficient as a model to describe the mechanism of the bc1 complex without invoking electron transfer across the dimer interface? Biochim. Biophis. Acta 1777. 1001-1019.
- Dikanov SA, Holland JT, Endeward B, Kolling DRJ, Samoilova RI, Prisner ThF, Crofts AR. 2007. Hydrogen bonds between nitrogen donors and the semiquinone in the Qi-site of the bc1 complex. J. Biol. Chem. 282: 25831-25841.
- Yap LL, Samoilova RI, Gennis RB, Dikanov SA. 2007. Characterization of mutants that change the hydrogen bonding of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli. J. Biol. Chem. 282: 8777-8785.
- Dikanov SA, Kolling DRJ, Endeward B, Samoilova RI, Prisner ThF, Crofts AR. 2006. Identification of hydrogen bonds to the Rieske cluster through the weakly coupled nitrogens detected by ESEEM spectroscopy. J. Biol. Chem. 281, 27416-27425.
- Shubin AA, Dikanov SA. 2006. The variations of g‑tensor principal values in reduced [2Fe‑2S] cluster of iron-sulfur proteins. Appl. Magn. Reson. 30, 399-416.
- Yap LL, Samoilova RI, Gennis RB, Dikanov SA. 2006. Characterization of the exchangeable protons in the immediate vicinity of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli. J. Biol. Chem. 281: 16879-16887.
- Iwasaki T, Kounosu K, Samoilova RI, Dikanov SA. 2006. 15N HYSCORE Characterization of the fully deprotonated, reduced form of the archaeal Rieske [2Fe-2S] Center. J. Am. Chem. Soc. 128: 2170-2171.
- Additional Publications
The major thrust of Dr. Dikanov's research activity is pulsed, high-resolution Electron Paramagnetic Resonance (EPR) spectroscopy and its applications as a structural tool in chemical and biomedical studies. During his previous work he has studied free radicals in irradiated solids, nitroxide radicals and biradicals in liquid and solid states, metal complexes and metal centers in metalloproteins, free radicals formed in primary photosynthetic reactions, and iron-sulfur proteins. His research involves collaboration withs chemists and biochemists around the world. His current and recent research projects include use of advanced EPR techniques to study structure-function relationships in Rieske-type metalloproteins, protein-semiquinone interactions in quinone processing sites of several proteins important for bioenergetics and photosynthesis, and binding of vanadium complexes that mimic insulin function to explore receptor sites in tissues.
Other Campus Affiliations
Illinois EPR Research Center
- Structure-function relationship in hyperthermostable, archaeal Rieske-type proteins.
- Theory and analysis methodology for two-dimansional Electron Spin Echo Envelope Modulation (ESEEM) powder spectra.
- NIH/NIGMS, Structure of reaction intermediates in the bc1 complex (Role: PI)
- DOE Energy Biosciences program, Mechanistic studies of catalysis in quinone electron transfer using high-resolution EPR (Role: PI)
- NIH/NCRR, Multifrequency pulsed Electron Paramagnetic Resonance spectrometer for biomedical studies (Role: PI)
- NSF, International Collaboration in Chemistry: Electronic structure of biological metallo-clusters and its magnetic interplay with the protein surrounding in thermophile metalloenzymes (Role: PI)
Honors and Awards
- Alexander von Humboldt Foundation Research Fellow Award
- Title: "Senior Research Scientist" from Russian Academy of Sciences
- USSR National Prize Winner for the development of high resolution EPR spectroscopy
S-, X- and Q-band pulsed EPR and ENDOR system