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The full list of my peer-reviewed publications is given below. Alternatively, it may be found in my Web Of Science Author Profile along with citation metrics and references to citing papers.


1.        Klinov, S.V., Davydov, D.R., Lisovskaya, N.P., Tarasov, O.S., and Kurganov, B.I. (1980) Kinetics of the interaction of muscle glycogen phosphorylase-B with glycogen.  Molecular Biology [Moscow] 14:270-277.

2.        Klinov, S.V., Chebotarieva, N.A., Lissovskaya, N.P., Davydov, D.R., and Kurganov, B.I. (1980) The interaction of muscle glycogen phosphorylase B with glycogen. Biochim. Biophys. Acta 709:91-98.

3.        Davydov, D.R. and Kurganov, B.I. (1982) Comparative investigation of the kinetics of the reduction of cytochrome P-450 by nadph-cytochrome-P-450 reductase and dithionite.  Biochemistry (Moscow) 47:1241-1247.

4.        Archakov, A.I., Borodin, E.A., Davydov, D.R., Karyakin, A.I., and Borovyagin, V.L. (1982) Random distribution of NADPH-specific flavoprotein and cytochrome P-450 in liver microsomes.  Biochem. Biophys. Res. Commun. 109:832-840.

5.        Davydov, D.R., Karyakin, A.V., Binas, B., Kurganov, B.I., and Archakov, A.I. (1985) Kinetic studies on reduction of cytochromes P-450 and b5 by dithionite. Eur. J. Biochem. 150:155-159.

6.        Kanaeva, I.P., Skotselyas, E.D., Turkina, I.F., Petrochenko, E.V., Davydov, D.R., Kondrashin, S.K., Dzuzenova, CH. S., Bachmanova, G.I., and Archakov, A.I. (1987) Reconstitution and catalytic properties of cytochrome P-450 LM2 in soluble system containing monomeric carriers.   Biochem. Biophys. Res. Commun. 147:1295-1299.

7.        Khailova, L.S., Kurganov, B.I., Nemerya, N.S., and Davydov, D.R. (1987) Pyruvate-dehydrogenase of pigeon pectoral muscle: Chemical modification of enzyme accompanied by conformational transition of protein.  Molecular Biology [Moscow] 21: 636-644.

8.        Kariakin, A.V., and Davydov, D.R. (1988) Kinetics of the electron transfer reaction of the monooxygenase system. Vestnik Akademii Meditsinskikh Nauk SSSR [Proc. Acad. Med. Sci., USSR, in Russian] 1:53-62.

9.        Kurganov, B.I., Shkarina, T.N., Malakhova, E.A., Davydov, D.R., and Chebotareva, N.A.  (1989) Kinetics of soybean lipoxygenase reaction in hydrated reversed micelles.  Biochimie 71:573-578.

10.      Shkarina, T.N., Malakhova, E.A., Kurganov, B.I., Davydov, D.R., and Chebotareva, N.A. (1989) Kinetics of the action of soybean lipoxygenase in hydrated reversed micelles. Biologicheskie Membrany [Russian] 6:362-371.

11.      Chebotareva, N.A., Kurganov, B.I, Liubarev, A.E., and Davydov, D.R. (1990) New approach to the study of binding of specific ligand by associating enzyme-system: Interaction of flavin mononucleotide with muscle glycogen phosphorylase-B. Doklady Akadenii Nauk SSSR [Proc. Acad. Sci USSR, in Russian] 313:235-237.

12.      Chebotareva, N.A., Kurganov, B.I., Lyubarev, A.E., Davydov, D.R., and Pekel, N.D. (1991) Interaction of flavin mononucleotide with dimeric and tetrameric forms of muscle phosphorylase -B.  Biochimie 73:1339-1343.

13.      Kurganov, B.I., Khailova, L.S., and Davydov, D.R. (1991) Kinetics of chemical   modification of oligomeric enzymes attended with conformational transitions of    subunits.  J. Chem.  Biochem. Kinetics 1:321-330.

14.      Davydov, D.R., Darovsky, B.V., Dedinsky, I.R., Kanaeva, I.P., Bachmanova, G.I., Blinov, V.M., and Archakov, A.I. (1992) Cytochrome c(Fe2+) as a competitive  inhibitor of NADPH- dependent reduction of cytochrome P450 LM2: locating protein-protein interaction sites in microsomal electron carriers. Arch. Biochem. Biophys. 297:304-313.

15.      Kanaeva, I.P., Nikityuk, O.V., Davydov, D.R., Dedinskii, I.R.; Koen, Y.M.; Kuznetsova, G.P., Skotselyas, E.D., Bachmanova, G.I., and Archakov, A.I. (1992) Comparative study of monomeric reconstituted and membrane microsomal monooxygenase systems of the rabbit liver. II. Kinetic parameters of reductase and monooxygenase reactions. Arch. Biochem. Biophys. 298:403-412.

16.      Davydov, D.R., Knyshko, T.V., and Hui Bon Hoa, G. (1992) High pressure induced inactivation of ferrous cytochrome P-450 LM2 (IIB4) CO-complex: Evidence for the presence of two conformers in the oligomer. Biochem. Biophys. Res. Commun. 188:216-221.

17.      Davydov, D.R., Erlikh, I., Klotz, E.E., and Fridman, V.G. (1992) A new method for recognition of structural and functional motifs in protein sequences based on the principal component analysis of profiles of physical-chemical properties. In: Mathematical Methods of Analysis of Byopolymer Sequences; DIMACS Series in Discrete Mathematics and Theoretical Computer Science, Vol. 8 (ed. S.Gindikin), American Mathematical Society, N.Y., 1992; p. 75-85.

18.      Jung, C., Hui Bon Hoa, G., Davydov, D.R., Gill, E., and Heremans, K. (1995) Compressibility of the heme pocket of substrate analogue complexes of cytochrome P-450cam-CO - The effect of hydrostatic pressure on the Soret band. Eur. J. Biochem. 233:600-606.

19.      Davydov, D.R., Deprez, E., Hui Bon Hoa, G., Knyushko, T.V., Kuznetsova, G.P., Koen, Y.M., and Archakov, A.I. (1995) High-pressure-induced transitions in microsomal cytochrome P450 2B4 in solution: Evidence for conformational inhomogeneity in the oligomers. Arch. Biochem. Biophys. 320:330-344.

20.      Renaud, J.-P., Davydov, D.R., Heirwegh, K.P.M., Mansuy, D., and Hui Bon Hoa, G. (1996) Thermodynamic studies of substrate binding  and spin transitions in human cytochrome P450 3A4 expressed in  yeast microsomes. Biochem. J., 319:675-681.

21.      Davydov, D.R., Knyushko, T.V., Kanaeva, I.P., Koen, Y.M., Samenkova, N.F., Archakov, A.I., and Hui Bon Hoa, G. (1996) Interactions of cytochrome P450 2B4 with NADPH-cytochrome P450 reductase studied by fluorescent probe - Biochime, 78:734-743.

22.      Davydov, D.R., Hui Bon Hoa, G. and Peterson, J.A. (1999) Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: Comparison with P450cam and P450 2B4. Biochemistry 38:751-761.

23.      Davydov, D.R., Kariakin, A.A., Petushkova, N.A., and Peterson, J.A. (2000) Association of cytochromes P450 with their reductases: opposite sign of the electrostatic interactions in P450 BM-3 as compared with the microsomal 2B4 system. Biochemistry 39:6489-6497.

24.      Davydov, D.R., Petushkova, N.A., Archakov, A.I., and Hui Bon Hoa, G. (2000) Stabilization of P450 2B4 by its association with P450 1A2 revealed by high-pressure spectroscopy.  Biochem. Biophys. Res. Commun. 276:1005-1012.

25.      Davydov, D.R. (2001) Microsomal monooxygenase in apoptosis: another target for cytochrome c signaling? Trends Biochem. Sci., 26:155-161.

26.      Davydov, D.R., Petushkova, N.A., Bobrovnikova, E.V., Knyushko, T.V., and Dansette, P. (2001) Association of cytochromes P450 1A2 and 2B4: are the interactions between different P450 species involved in the control of the monooxygenase activity and coupling? Adv. Exp. Med. Biol. 500:335-338.

27.   Davydov, D.R., Kumar, S., and Halpert, J.R. (2002) Allosteric mechanisms in P450eryF probed with 1-pyrenebutanol, a novel fluorescent substrate. Biochem Biophys Res. Commun. 294:806-812.

28.    Kariakin, A., Davydov, D., Peterson, J.A., and Jung, C. (2002) A new approach to the study of protein-protein interaction by FTIR: Complex formation between cytochrome P450BM3 heme domain and FMN reductase domain. Biochemistry 41:13514-13525.

29.     Davydov, D.R., Halpert, J.R., Renaud J.-P., Hui Bon Hoa, G. (2003) Conformational heterogeneity of cytochrome P450 3A4 revealed by high-pressure spectroscopy. Biochem.Biophys.Res.Commun.,312,121-130.

30.      Zangar, R. C., Davydov, D.R., Verma, S. (2004) Mechanisms that regulate production of reactive oxygen species by cytochrome P450 Toxicology & Applied Pharmacology, 119, 316-334

31.      Davydov, D.R.,  Botchkareva AE.,  Kumar S.,  He YQ.,  and Halpert JR. (2004) An Electrostatically Driven Conformational Transition Is Involved in the Mechanisms of Substrate Binding and Cooperativity in Cytochrome P450eryF. Biochemistry.  43(21):6475-85.

32.      Davydov, D.R., Botchkareva E.B., Davydova N.E., Halpert J.R. (2005) Resolution of Two Substrate-Binding Sites in an Engineered Cytochrome P450eryF Bearing a Fluorescent Probe. Biophys. J., 89(1):418-432

33.       Kumar, S.; Davydov, D.R.; and Halpert, J.R. (2005) Role of Cytochrome b5 in modulating peroxide-supported CYP3A4 activity: evidence for a conformational transition and P450 heterogeneity. Drug Metab. Disp., 33(8):1131-1136.

34.      Davydov, D.R.; Fernando, H.; Baas, B.J.; Sligar, S.G.; Halpert, J.R. (2005) Kinetics of dithionite-dependent reduction of cytochrome P450 3A4:Heterogeneity of the enzyme caused by its oligomerization. Biochemistry,  44(42):13902-13913

35.      Davydov, D.R.; Fernando, H.; Halpert, J.R. (2006) Variable path length and counter-flow continuous variation methods for the study of the formation of high-affinity complexes by absorbance spectroscopy. An application to the studies of substrate binding in cytochrome P450. Biophys. Chem.,  123,  95-101.

36.      Fernando, H.; Halpert, J.R.; Davydov, D.R. (2006) Resolution of multiple substrate binding sites in cytochrome P450 3A4: The stoichiometry of the enzyme-substrate complexes probed by FRET and Job's titration. Biochemistry,  45 (13), 4199-4209.

37.     Tsalkova, T.N., Davydova, N.E., Halpert, J.R., Davydov, D.R. (2007) Mechanism of interactions of alpha-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe. Biochemistry,  46 (1), 106-119

38.      Fernando, H., Davydov, D.R., Chin, C. C., and Halpert, J. R. (2007) Role of subunit interactions in P450 oligomers in the loss of homotropic cooperativity in the cytochrome P450 3A4 mutant L211F/D214E/F304W, Arch. Biochem. Biophys. 460, 129-140.

39.      Davydov, D.R., Baas, B.J., Sligar, S.G., Halpert, J.R. (2007) Allosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket. Biochemistry 46, 7852-7864

40.        Fernando, H., Halpert, J.H., Davydov, D.R. (2007) Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein. Arch. Biochem. Biophys. 471, 20–31

41.      Davydov, D.R.; Davydova, N.Y.; Tsalkova, T.N.; Halpert, J.R. (2008) Effect of glutathione on homo- and heterotropic cooperativity in cytochrome P450 3A4 – Arch. Biochem. Biophys., 471 (2), 134-145.

42.      Davydov, D.R.; Davydova, N.Y.; Halpert, J.R.; Davydova N. Y.; Halpert, J. R. (2008) Allosteric transitions in cytochrome P450eryF explored with pressure-perturbation spectroscopy, lifetime FRET, and a novel fluorescent substrate, Fluorol-7GA -  Biochemistry,  47 (43), 11348-11359. 

43.      Davydov, D.R.; Halpert, J.R. (2008) Allosteric P450 mechanisms: multiple binding sites, multiple conformers or both? -  Expert Opinion Drug Metab. Toxicol., 4 (2), 1523-1535.

44.        Davydov, D.R.; Sineva, E.V.; Sistla, S.; Davydova, N.Y.; Frank, D.J.; Sligar, S.G.; Halpert, J.R. (2010) Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: The effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium -  Biochim. Biophys. Acta Bioenergetics,  1797 (3),  378-390

45.     Sineva, E.V.; Davydov, D.R. (2010) Cytochrome P450 from Photobacterium profundum SS9, a piezophilic bacterium, exhibits tightenedcontrol of water access to the active site -  Biochemistry,  49 (50),  10636-10646.

46.      Sineva, E.V.; Davydov, D.R. (2010) Constrained water access to the active site of cytochrome P450 from the piezophilic bacterium Photobacterium profundum – High Pressure Res.,  30 (4),  466-474.

47.      Talakad, J.C.; Wilderman, P.R.; Davydov, D.R.; Kumar, S.; Halpert, J.R. (2010) Rational engineering of cytochromes P450 2B6 and 2B11 for enhanced stability: Insights into structural importance of residue 334 -  Arch. Biochem. Biophys.,  494 (2),  151-158.

48.      Davydov, D.R. (2011) Microsomal monooxygenase as a multienzyme system: the role of P450-P450 interactions -  Expert Opinion Drug Metabolism and Toxicology,  7 (5),  543-558.

49.      Fernando, H.; Rumfeldt, J.A.O.; Davydova, N.Y.; Halpert, J.R.; Davydov, D.R. ( 2011) Multiple substrate-binding sites are retained in cytochrome P450 3A4 mutants with decreased cooperativity -  Xenobiotica,  41 (4),  281-289.

50.      Davydov, D.R.; Rumfeldt, J.A.O.; Sineva, E.V.; Fernando, H.; Davydova, N.Y.; Halpert, J.R. (2012) Peripheral ligand-binding site in cytochrome P450 3A4 located with fluorescence resonance energy transfer (FRET) -  J. Biol. Chem.,  287 (9),  6797-6809.

51.      Davydov, D.R. (2012) Merging thermodynamics and evolution: how the studies of high-pressure adaptation may help to understand enzymatic mechanisms (editorial) - J. Thermodynam. Cat., 3, e110 (doi: 10.4172/2157-7544.1000e110).

52.      Davydov, D.R., Sligar S.G. (2013) In memoriam of Bill Peterson (editorial) - Biotechnology and Applied Biochemistry, 60 (1), 2-3

53.      Davydov, D.R.; Sineva, E.V.; Davydova, N.Y.; Bartlett, D.H.; Halpert, J.R. (2013) CYP261 enzymes from deep sea bacteria: a clue to conformational heterogeneity in cytochromes P450. Biotechnology and Applied Biochemistry, 60 (1) 30-40.

54.      Davydov, D.R.; Ponomarev, G.V.; Bobrovnikova-Marjon, E.; Haines, D.C.; Peterson, J.A. (2013) Aluminum-substituted heme domain of P450BM-3 (BMP): introducing a heme-derived fluorescent probe for the studies of substrate binding and protein-protein interactions in cytochromes P450. Biotechnology and Applied Biochemistry. 60 (1) 41-51.

55.      Davydov, D.R., Davydova, N. Y., Sineva, E. V., Kufareva, I. and Halpert, J. R. (2013) Pivotal role of P450–P450 interactions in CYP3A4 allostery: the case of α-naphthoflavone. - Biochem. J. 453 (2), 219-230

56.      Sineva, E.V., Rumfeldt, J.A.O., Halpert, J.R., and Davydov, D.R. (2013) A large-scale allosteric transition in cytochrome P450 3A4 revealed by luminescence resonance energy transfer (LRET) PLOS One, 8 (12), e83898 (DOI: 10.1371/journal.pone.0083898).

57.      Jang, H.H., Davydov, D.R., Lee, G.Y., Yun CH, Halpert J.R. (2014) The role of cytochrome P450 2b6 and 2b4 substrate access channel residues predicted based on crystal structures of the amlodipine complexes. Arch. Biochem. Biophys., 545, 100–107

58.     Muller, C.S., Knehans, T., Davydov, D.R., Bounds, P.L., von Mandach, U., Halpert, J.R., Caflisch, A., Koppenol, W.H. (2015) Concurrent cooperativity and substrate inhibition in the epoxidation of carbamazepine by cytochrome P450 3A4 active site mutants inspired by molecular dynamics simulations. Biochemistry 54(3) 711- 721

59.     Davydov, D.R., Davydova, N.Y., Sineva, E.V. and Halpert, J.R. (2015) Interactions among Cytochromes P450 in Microsomal Membranes: Oligomerization of Cytochromes P450 3A4, 3A5 and 2E1 and its Functional Consequences. J. Biol.Chem., 453, 219-230.

60.      Davydov, D.R. (2015) Molecular organization of the microsomal oxidative system: a new connotation for an old term. Biochemistry (Moscow), Suppl. B., 2016, 10 (1), 10-21

61.       Davydov, D.R., Yang, Z.Y., Davydova, N., Halpert, J.R., Hubbell, WL (2016)  Conformational mobility in cytochrome P450 3A4 explored by pressure-perturbation EPR spectroscopy, Biophys. J., 110 (7), 1485-1498

62.      Davydov, D.R., Davydova, N.Y., Rodgers, J.T., Rushmore, T.H., and Jones, J.P.(2017) Toward a systems approach to the human cytochrome P450 ensemble: interactions between CYP2D6 and CYP2E1 and their functional consequences. Biochem. J. 474, 3523-3542

63.      Rodgers, J.T., Davydova, N.Y., Paragas, E.M., Jones, J.P., and Davydov, D.R. (2018) Kinetic mechanism of time-dependent inhibition of CYP2D6 by 3,4-methylenedioxymethamphetamine (MDMA): Functional heterogeneity of the enzyme and the reversibility of its inactivation. Biochem. Pharm., 156, 86-98

64.   Davydova, N. Y., Dangi, B., Maldonado, M. A., Vavilov, N. E., Zgoda, V. G., and Davydov, D. R. (2019) Toward a systems approach to cytochrome P450 ensemble: interactions of CYP2E1 with other P450 species and their impact on CYP1A2, Biochem J. 476, 3661-3685.

65.    Gerringer ME, Yancey PH, Tikhonova OV, Vavilov NE, Zgoda VG, Davydov DR. (2020) Pressure tolerance of deep-sea enzymes can be evolved through increasing volume changes in protein transitions: a study with lactate dehydrogenases from abyssal and hadal fishes. FEBS J., 287, 5394-5410

66.    Zhang B, Lewis KM, Abril A, Davydov DR, Vermerris W, Sattler SE, Kang C. (2020). Structure and Function of the Cytochrome P450 Monooxygenase, Cinnamate 4-hydroxylase (C4H1) from Sorghum bicolor. Plant Physiology, 183, 957-973

67.    Dangi, B., Davydova, N.Y., Vavilov, N.E., Zgoda, V.G. and Davydov, D.R. (2020) Nonadditivity in Human Microsomal Drug-Metabolizing Ensemble Revealed with Coumarin-152, a Polyspecific Cytochrome P450  Substrate, Xenobiotica, 50, 1393-1405 

68.    Dangi, B., Davydova, N. Y., Maldonado, M.A., Abbasi, A., Vavilov, N. E., Zgoda, V. G. and Davydov, D. R. (2021) Effects of alcohol-induced increase in CYP2E1 content in human liver microsomes on the activity and cooperativity of CYP3A4, Arch. Biochem. Biophys., 698, 108677

69.   Dangi, B., Davydova, N. Y., Maldonado, M. A., Ahire, D., Prasad, B., and Davydov, D. R. (2021) Probing functional interactions between cytochromes P450 with principal component analysis of substrate saturation profiles and targeted proteomics, Arch Biochem Biophys 708, 108937

70.   Davydov, D.R., Prasad B. (2021) Assembling the P450 puzzle: on the sources of nonadditivity in drug metabolism, Trends Pharm Sci 42, 988-997

71.   Davydov, D. R., Dangi, B., Yue, G., Ahire, D. S., Prasad, B., and Zgoda, V. G. (2022) Exploring the Interactome of Cytochrome P450 2E1 in Human Liver Microsomes with Chemical Crosslinking Mass Spectrometry, Biomolecules 12, 185

72.  Zhang, B.X.; Kang, C.; Davydov, D.R. (2022) Conformational Rearrangements in the Redox Cycling of NADPH-Cytochrome P450 Reductase from Sorghum bicolor Explored with FRET and Pressure-Perturbation Spectroscopy. Biology-Basel 2022, 11,

73.   Zhang, B.X.; Munske, G.R.; Timokhin, V.I.; Ralph, J.; Davydov, D.R.; Vermerris, W.; Sattler, S.E.; Kang, C. (2022) Functional and structural insight into the flexibility of cytochrome P450 reductases from Sorghum bicolor and its implications for lignin composition. J. Biol. Chem. 2022, 298

74.   Davydova, N.Y.; Hutner, D.A.; Gaither, K.A.; Singh, D.K.; Prasad, B.; Davydov, D.R. (2023) High-throughput assay of cytochrome P450-dependent drug demethylation reactions and Its use to re-evaluate the pathways of ketamine metabolism. Biology-Basel 2023, 12