The group of Professor of the Russian Academy of Sciences (RAS), Ph.D., D.Sc., Principal Investigator Vitaliy B. Borisov is engaged in a comprehensive study of quinol oxidases of bacterial respiratory chains using modern biochemical and biophysical methods.
The main research directions include the elucidation of the molecular mechanism of functioning and the physiological role of quinol oxidases of bacterial respiratory chains (cytochromes bd and bo). These key components of the respiratory chains of prokaryotes can couple the oxidation of quinol by oxygen with the generation of proton-motive force. We are engaged in the identification of the unique features of quinol oxidases that allow them to combine energy conservation with the performance of other, alternative functions that are important for the survival, growth, and reproduction of bacterial cells. We are studying the resistance of quinol oxidases to a number of low-molecular-weight and physiologically active compounds; investigating the ability of enzymes to metabolize some of these compounds; elucidating the mechanisms of the generation of proton-motive force and the organization of cytochrome active sites for oxygen reduction; examining the main intermediates of the catalytic cycle of enzymes. New knowledge about the structural and functional properties of prokaryotic quinol oxidases and their differences from the properties of the terminal oxidase in humans and animals will contribute to the development of new pharmaceutical preparations against microbial infections in which these bacterial proteins serve as a therapeutic target.
Upon studies of bd-type quinol oxidases (E. coli cytochrome bd), for the first time, the rapid kinetics of membrane potential generation and sequential formation of spectrally distinguishable catalytic intermediates within one molecular turnover were recorded; data on the existence of an intraprotein proton-conducting pathway were obtained; femto-, pico-, and microsecond dynamics of enzyme's active site were established, and a fast electron transfer between the hemes was revealed; the affinity of heme d for oxygen was determined. It was found for the first time that the bd-type quinol oxidase endows E. coli with resistance to nitric oxide and hydrogen sulfide, and is also capable of metabolizing hydrogen peroxide and peroxynitrite.
Collaboration with the Sapienza University of Rome (Italy), the Kyushu Institute of Technology (Japan), the University of Sheffield (UK), the University of Illinois at Urbana-Champaign (USA), the University of Helsinki (Finland).
The studies were supported by grants from the Russian Foundation for Basic Research (№ 99-04-48095, 02-04-48314, 05-04-48096, 08-04-00093, 11-04-00031, 14-04-00153, 19-04-00094).
Vitaliy B. Borisov is a lecturer of the annual course "Biochemistry" at the Faculty of Bioengineering and Bioinformatics of Lomonosov Moscow State University (since 2005).
State Prize Award for young scientists (1999), Award of the Biochemical Society of Russia for young scientists (2000), Kaulen Award for young scientists for the best research in Belozersky Institute (2000), Award of the Russian Higher Education Academy of Sciences for young scientists (2000), Award for young scientists for the best research in Lomonosov Moscow State University (2001), Academia Europaea Prize for Young Russian Scientists (2002), Shuvalov Award of Lomonosov Moscow State University (2007).