Attraction of the leading scientists to Russian institutions of higher learning, research organizations of the governmental academies of sciences, and governmental research centers of the Russian Federation

Laboratory for Magnetic Resonance of Biomolecular Systems

About laboratory

Direction (topic) of the scientific research project: Multifrequency electron paramagnetic resonance (EPR) for biochemical research

Grant Agreement No.:

Name of the institution of higher learning: N.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry of Siberian Branch of Russian Academy of Sciences

Fields of scientific research: Chemistry

This project is aimed at application of modern cutting-edge EPR technologies for topical tasks in biochemistry. EPR is a powerful tool for studying chemically, biologically and physically-relevant systems containing paramagnetic centers.

Leading scientist

 Bowman

Michael K. Bowman

 

Citzenship: USA

Job Title: Professor of Chemistry, The University of Alabama

Academic degree and title: Prof., Ph.D.

Field of scientific interests: Electron Paramagnetic Resonance; Spin Relaxation; Biophysics; Electron Transfer

Academic recognition:

Professor Bowman has been a consistent leader in the development and application of pulsed EPR spectroscopy for:
• Developed the first computer-controlled pulsed EPR spectrometer, 1980
• Characterization of iron containing enzymes by HYSCORE and pulsed EPR, 1996
• Determined mechanism of metal inhibition of cytochrome b6f enzymes, 2002
• Characterized the novel heme x in cytochrome b6f, 2004
• Determined the solution structure of trityl radicals, 2005
• Trapped and characterized the semiquinone intermediate in cytochrome bc1 enzymes by EPR, 2007
• Measured structural responses of catalytic RNA structures to metal ions, 2010
• Discovered a novel binding mode for type-II inhibitors of P450 enzymes, 2012
• Developed a new pulsed EPR method for oxymetric EPR imaging, 2013
• Determined the location of enzymmatic intermediates in cytochrome bc1 and nitric oxide synthase by EPR relaxation, 2013
• Characterized the properties of self-assembled aggregates of trityl radicals in dynamic nuclear polarization, 2015

1. Bowman MK, Chen H, Maryasov AG. Fourier-Transform EPR. In: Goldfarb D, Stoll S, editors. Emagres. 6. 15 SEP 2017 ed. Chichester: John Wiley & Sons, Ltd; 2017. p. 387-406.

2. Lockart MM, Rodriguez CA, Atkins WM, Bowman MK. CW EPR parameters reveal cytochrome P450 ligand binding modes. J Inorg Biochem. 2018;183:157-64.

3. Chen H, Maryasov AG, Rogozhnikova OY, Trukhin DV, Tormyshev VM, Bowman MK. Electron spin dynamics and spin-lattice relaxation of trityl radicals in frozen solutions. PCCP. 2016;18(36):24954-65.

4. Trukhin DV, Rogozhnikova OY, Troitskaya TI, Vasiliev VG, Bowman MK, Tormyshev VM. Facile and High-Yielding Synthesis of TAM Biradicals and Monofunctional TAM Radicals. Synlett. 2016;27(6):893-9.

5. Krzyaniak MD, Cruce AA, Vennam P, Lockart M, Berka V, Tsai AL, et al. The tetrahydrobiopterin radical interacting with high- and low-spin heme in neuronal nitric oxide synthase - A new indicator of the extent of NOS coupling. Free Radic Biol Med. 2016;101:367-77.

6. Conner KP, Schimpf AM, Cruce AA, McLean KJ, Munro AW, Frank DJ, et al. Strength of Axial Water Ligation in Substrate-Free Cytochrome P450s Is Isoform Dependent. Biochemistry. 2014;53(9):1428-34.

7. Epel B, Bowman MK, Mailer C, Halpern HJ. Absolute Oxygen R-1e Imaging In Vivo with Pulse Electron Paramagnetic Resonance. Magn Reson Med. 2014;72(2):362-8.

8. Trukhan SN, Yudanov VF, Tormyshev VM, Rogozhnikova OY, Trukhin DV, Bowman MK, et al. Hyperfine interactions of narrow-line trityl radical with solvent molecules. J Magn Reson. 2013;233:29-36.

9. Vennam PR, Fisher N, Krzyaniak MD, Kramer DM, Bowman MK. A Caged, Destabilized, Free Radical Intermediate in the Q-Cycle. ChemBioChem. 2013;14(14):1745-53.

10. Conner KP, Vennam P, Woods CM, Krzyaniak MD, Bowman MK, Atkins WM. 1,2,3-Triazole-Heme Interactions in Cytochrome P450: Functionally Competent Triazole-Water-Heme Complexes. Biochemistry. 2012;51(32):6441-57.

11. Kim NK, Bowman MK, DeRose VJ. Precise mapping of RNA tertiary structure via nanometer distance measurements with double electron-electron resonance spectroscopy. J Am Chem Soc. 2010;132(26):8882-4.

12. Cape JL, Bowman MK, Kramer DM. A semiquinone intermediate generated at the Qo site of the cytochrome bc1 complex: importance for the Q-cycle and superoxide production. P Natl Acad Sci USA. 2007;104(19):7887-92.

13. Cape JL, Bowman MK, Kramer DM. Understanding the cytochrome bc complexes by what they don't do. The Q-cycle at 30. Trends Plant Sci. 2006;11(1):46-55.

14. Bowman MK, Mailer C, Halpern HJ. The solution conformation of triarylmethyl radicals. J Magn Reson. 2005;172(2):254-67.

15. Halpern HJ, Jaffe DR, Nguyen TD, Haraf DJ, Spencer DP, Bowman MK, et al. Measurement of bioreduction rates of cells with distinct responses to ionizing radiation and cisplatin. Biochim Biophys Acta. 1991;1093 (2-3):121-4.

16. Isoya J, Kanda H, Norris JR, Tang J, Bowman MK. Fourier-transform and continuous-wave EPR studies of nickel in synthetic diamond: Site and spin multiplicity. Phys Rev B Condens Matter. 1990;41(7):3905-13.

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