1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase

Journal of Biomolecular NMR

Volumn 10, Issue 1, 1997, Pages 63-75

  Barsukov, Igor ^a   Modi, Sandeep ^a   Lian, Lu Yun ^a   Sze, Kong Hung ^a   Paine, Mark J I ^b   Wolf, C Roland ^b   Roberts, Gordon C K ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

^b UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

Cytochrome P450 reductase; Flavin mononucleotide; Resonance assignment; Semiautomatic; Triple resonance

Indexed keywords

CARBON; FLAVINE MONONUCLEOTIDE; HYDROGEN; NITROGEN; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; COMPUTER SIMULATION; ENZYMOLOGY; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SKIN;

AMINO ACID SEQUENCE; BINDING SITES; CARBON RADIOISOTOPES; COMPUTER SIMULATION; FLAVIN MONONUCLEOTIDE; HUMANS; HYDROGEN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADPH-FERRIHEMOPROTEIN REDUCTASE; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SKIN;

EID: 0031173906     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1018313830207     Document Type: Article

References (43)

1. Backes, W.L. (1993) Handbook Exp. Pharmacol., 105, 15-34.
2. Burnett, R.M., Darling, G.D., Kendall, D.S., LeQuesne, M.E., Mayhew, S.G., Smith, W.W. and Ludwig, M.L. (1974) J. Biol. Chem., 249, 4383-4392.
3. Clubb, R.T., Thanabal, V. and Wagner, G. (1992) J. Magn. Reson., 97, 213-217.
4. Djordjevic, S., Roberts, D.L., Wang, M., Shea, T., Camitta, M.G.W., Masters, B.S.S. and Kim, J.J.P. (1995) Proc. Natl. Acad. Sci. USA, 92, 3214-3218.
5. Edmondson, D.E. and Tollin, G. (1971) Biochemistry, 10, 124-132.
6. Friedrichs, M.S., Mueller, L. and Wittekind, M. (1994) J. Biomol. N M R, 4, 703-726.
7. Fukuyama, K., Matsubara, H. and Rogers, L.J. (1992) J. Mol. Biol., 225, 775-789.
8. Genzor, C.G., Perales-Alcón, A., Sancho, J. and Romero, A. (1996) Nat. Struct. Biol., 3, 329-332.
9. Griffey, R.H., Redfield, A.G., Loomis, R.E. and Dahlquist, F.W. (1985) Biochemistry, 24, 817-822.
10. Grzesiek, S. and Bax, A. (1992a) J. Magn. Reson., 96, 432-440.
11. Grzesiek, S. and Bax, A. (1992b) J. Magn. Reson., 99, 201-207.
12. Iyanagi, T. and Mason, H.S. (1973) Biochemistry, 13, 1701-1710.
13. Kay, L.E., Keifer, P. and Saarinen, T. (1992) J. Am. Chem. Soc., 114, 10663-10665.
14. Keyse, S.R., Fracasso, P.M., Heimbrook, D.C., Rockwell, S., Sligar, S.G. and Sartorelli, A.C. (1984) Cancer Res., 44, 5638-5643.
15. Kim, J.J.P., Wang, M., Roberts, D.L., Paschke, R., Shea, T. and Masters, B.S.S. (1996) XIth International Symposium on Microsomes and Drug Oxidation, University of California, Los Angeles, CA, U.S.A.
16. Knauf, M.A., Löhr, F., Blümel, M., Mayhew, S.G. and Rüterjans, H. (1996) Eur. J. Biochem., 238, 423-434.
17. Kurzban, G.P., Howarth, J., Palmer, G. and Strobel, H.W (1990) J. Biol. Chem., 265, 12272-12279.
18. Lu, A.Y.H., Junk, K.W. and Coon, M.J. (1969) J. Biol. Chem., 244, 3714-3721.
19. Majumdar, A., Wang, H., Morshauser, R.C. and Zuiderweg, E.R.P. (1993) J. Biomol. N M R, 3, 387-397.
20. Muhandiram, D.R. and Kay, L.E. (1994) J. Magn. Reson., B103, 203-216.
21. Narayanasami, R., Otvos, J.D., Kasper, C.B., Shen, A., Rajagopalan, J., McCabe, T.J., Okita, J.R., Hanahan, D.J. and Masters, B.S.S. (1992) Biochemistry, 31, 4210-4218.
22. Pascal, S.M., Muhandiram, D.R., Yamazaki, T., Forman-Kay, J.D. and Kay, L.E. (1994) J. Magn. Reson., B103, 197-201.
23. Peelen, S. and Vervoort, J. (1994) Arch. Biochem. Biophys., 314, 291-300.
24. Peelen, S., Wijmenga, S.S., Erbel, P.J.A., Robson, R.L., Eady, R.R. and Vervoort, J. (1996) J. Biomol. N M R, 1, 315-330.
25. Phillips, A.H. and Langdon, R.G. (1962) J. Biol. Chem., 237, 2652-2660.
26. Piotto, M., Saudek, V. and Sklenář, V. (1992) J. Biomol. NMR, 2, 661-665.
27. Porter, T.D. and Kasper, C.B. (1986) Biochemistry, 25, 1682-1687.
28. Porter, T.D. (1991) Trends Biochem. Sci., 16, 154-158.
29. Rao, S.T., Shaffie, F., Yu, C., Satyshur, K.A., Stockman, B.J. and Sundaralingam, M. (1992) Protein Sci., 1, 1413-1427.
30. Romero, A., Caldeira, J., LeGall, J., Moura, I., Moura, J.J.G. and Romao, M.J. (1996) Eur. J. Biochem., 239, 190-196.
31. Sali, A. and Blundell, T.L. (1993) J. Mol. Biol., 234, 779-815.
32. Sevrioukova, I. and Peterson, J.A. (1995) Biochimie, 77, 562-572.
33. Sevrioukova, I., Shaffer, C., Ballou, D.P. and Peterson, J.A. (1996) Biochemistry, 35, 7058-7068.
34. Smith, G.C.M., Tew, D.G. and Wolf, C.R. (1994) Proc. Natl. Acad. Sci. USA, 91, 8710-8714.
35. Stockman, B.J., Euvrard, A., Kloosterman, D.A., Scahill, T.A. and Swenson, R.P. (1993) J. Biomol. N M R, 3, 133-149.
36. Strobel, H.W., Hodgson, A.V. and Shen, S. (1995) In Cytochrome P450: Structure, Mechanism and Biochemistry, 2nd ed. (Ed., Ortiz de Montellano, P.R.), Plenum, New York, NY, U.S.A., pp. 225-244.
37. Vuister, G.W., Clore, G.M., Gronenborn, A.M., Powers, R., Garrett, D.S., Tshudin, R. and Bax, A. (1993) J. Magn. Reson., B101, 210-213.
38. Walton, M.I., Wolf, C.R. and Workman, P. (1992) Biochem. Pharmacol., 44, 251-259.
39. Watt, W., Tulinsky, A., Swenson, R.P. and Watenpaugh, K.D. (1991) J. Mol. Biol., 218, 195-208.
40. Williams, C.H. and Kamin, H. (1962) J. Biol. Chem., 237, 587-595.
41. Wishart, D.S. and Sykes, B.D. (1994) J. Biomol. N M R, 4, 171-180.
42. Zhang, O., Kay, L.E., Oliver, J.P. and Forman-Kay, J.D. (1994) J. Biomol. N M R, 4, 845-858.
43. Zhao, Q., Smith, G., Paine, M., Wolf, C.R., Tew, D., Modi, S., Lian, L.-Y., Primrose, W.U., Roberts, G.C.K. and Driessen, H. (1996) J. Struct. Biol., 116, 320-325.