The interaction of cytochrome P450 17α with NADPH-cytochrome P450 reductase, investigated using chemical modification and MALDI-TOF mass spectrometry

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 6, 2006, Pages 1126-1131

  Nikfarjam, Laleh ^a   Izumi, Shunsuke ^b   Yamazaki, Takeshi ^a   Kominami, Shiro ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

^b HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Chemical modification; Cytochrome P450; MALDI TOF mass spectrometry; NADPH cyrochrome P450 reductase; Protein protein interaction

Indexed keywords

ACETIC ANHYDRIDE; CYTOCHROME P450 17; CYTOCHROME P450 17ALPHA; LYSINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; ENZYME ACTIVITY; ENZYME INACTIVATION; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; REACTION TIME; TEMPERATURE DEPENDENCE;

ANIMALS; GUINEA PIGS; LYSINE; MODELS, MOLECULAR; NADPH-FERRIHEMOPROTEIN REDUCTASE; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STEROID 17-ALPHA-HYDROXYLASE; TEMPERATURE;

CAVIA PORCELLUS;

EID: 33745200715     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.04.003     Document Type: Article

References (34)

1. Kominami S., Hara H., Ogishima T., and Takemori S. Interaction between cytochrome P450 (P450 C21) and NADPH-cytochrome P450 reductase from adrenal microsomes in a reconstituted system. J. Biol. Chem. 259 (1984) 2991-2999
2. Shen S., and Strobel H.W. The role of cytochrome P450 lysine residues in the interaction between cytochrome P450IA1 and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 294 (1992) 83-90
3. Bridges A., Gruenke L., Chang Y.T., Vasker I.A., Loew G., and Waskell L. Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase. J. Biol. Chem. 273 (1998) 17036-17049
4. Shimada T., Mernaugh R.L., and Guengerich F.P. Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b5 enzymes. Arch. Biochem. Biophys. 435 (2005) 207-216
5. Steiner R.F., Albaugh S., Fenselau C., Murphy C., and Vestling M. A mass spectrometry method for mapping the interface topography of interaction proteins, illustrated by the mellitin-calmodulin system. Anal. Biochem. 196 (1991) 120-125
6. Suckau D., Mak M., and Przybylski M. Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 5630-5634
7. Izumi S., Kaneko H., Yamazaki T., Hirata T., and Kominami S. Membrane topology of Guinea pig cytochrome P45017α revealed by a combination of chemical modification and mass spectrometry. Biochemistry 42 (2003) 14663-14669
8. Hager-Braun C., and Tommer K.B. Characterization of the tertiary structure of soluble CD4 bound to glycosilated full-length HIV gp 120 by chemical modification of arginine residues and mass spectrometric analysis. Biochemistry 41 (2002) 1759-1766
9. Shell S.M., Hess S., Kvaratskhelia M., and Zou Y. Mass spectrometric identification of lysines involved in the interaction of human replication protein with a single-stranded DNA. Biochemistry 44 (2005) 971-978
10. Yamazaki T., Ohno T., Sakaki T., Akiyoshi-shibata M., Yabusaki Y., Imai T., and Kominami S. Kinetic analysis of successive reactions catalyzed by bovine cytochrome P450 17α. Biochemistry 37 (1998) 2800-2806
11. Omura T., and Sato R. The carbon monoxide-binding pigment of liver microsomes. J. Biol. Chem. 239 (1964) 2379-2385
12. Yasukochi Y., and Masters B.S. Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. J. Biol. Chem. 251 (1976) 5337-5344
13. French J.S., and Coon M.J. Properties of NADPH-cytochrome P450 reductase purified from rabbit liver microsomes. Arch. Biochem. Biophys. 195 (1979) 565-577
14. Gharadaghi F., Weinberg C.R., Meagher D.A., Imai B.S., and Mische S.M. Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis 20 (1999) 601-605
15. Higuchi A., Kominami S., and Takemori S. Kinetic control of steroidogenesis by steroid concentration in guinea pig adrenal microsomes. Biochim. Biophys. Acta 1084 (1991) 240-246
16. Fojo F.T., Reuben P.M., Whitney P.L., and Awad Jr. W.M. Effect of glycerol on protein acetylation by acetic anhydride. Arch. Biochem. Biophys. 240 (1985) 43-50
17. Stratilova E., Dzurova M., Markovic O., and Jornvall H. An essential tyrosine residue of Aspergillus polygalacturanase. FEBS Lett. 382 (1996) 164-166
18. Macdonald J.M., Hass A.L., and London R.E. Novel mechanism of surface catalysis of protein adduct formation. J. Biol. Chem. 275 (2000) 31908-31913
19. Shen S., and Strobel H.W. Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 304 (1993) 257-265
20. Tamburini P.P., and Schenkman J.B. Differences in the mechanism of functional interaction between NADPH-cytochrome P450-reductase and its redox partners. Mol. Pharmacol. 30 (1986) 178-185
21. 17α,lyase) from guinea pig adrenal microsomes. Dual function of a single enzyme and effect of cytochrome b5. Biochim. Biophys. Acta 833 (1985) 151-160
22. Bernhardt R., Pommerening K., and Ruckpaul K. Modification of carboxyl groups on NADPH-cytochrome P450 reductase involved in binding of cytochrome c and P450LM2. Biochem. Int. 14 (1987) 823-832
23. Nadler S.G., and Strobel H.W. Role of electrostatic interactions in the reaction of NADPH-cytochrome P450-reductase with cytochromes P450. Arch. Biochem. Biophys. 261 (1988) 418-429
24. Auchus R.J., and Miller W.L. Molecular modeling of human P450c17 (17α-hydroxylase/ 17, 20-lyase): insights into reaction mechanisms and effect of mutations. Mol. Endocrinol. 13 (1999) 1169-1182
25. Bernhardt R., Kraft K., Otto A., and Ruckpaul K. Electrostatic interactions between cytochrome P450 LM2 and NADPH-cytochrome P450-reductase. Biomed. Biochim. Acta 7 (1988) 581-592
26. Geller D.H., Auchus R.J., and Miller W.L. P450c17 mutations R347H and R358Q selectively disrupt 17, 20-lyase activity by disrupting interactions with P450 oxidoreductase and cytochrome b5. Mol. Endocrinol. 13 (1999) 167-175
27. Costa-Santos M., Kater C.E., and Auchus R.J. Two prevalent CYP17 mutations and genotype-phenotype correlations in 24 Brazilian patients with 17-hydroxylase deficiency. J. Clin. Endocrinol. Metab. 89 (2004) 49-60
28. Lee-Robichaud P., Akhtar M.E., Wright J.N., Sheikh Q.I., and Akhtar M. The cationic charges on Arg347, Arg358 and Arg449 of human CYP17 are essential for enzyme's cytochrome b5-dependent acyl-carbon cleavage activities. J. Steroid Biochem. Mol. Biol. 92 (2004) 119-130
29. Miguel R.N., Chen S., Nikfarjam L., Kominami S., Carpenter B., Dal Pra C., Betterle C., Zanchetta R., Nakamatsu T., Powell M., Hewer R., Blundell T.L., Smith B.R., and Furmaniak J. Analysis of the interaction between human steroid 21-hydroxylase and various monoclonal antibodies using comparative structural modeling. Eur. J. Endocrinol. 153 (2005) 949-961
30. Gum J.R., and Strobel H.W. Isolation of the membrane-binding peptide of NADPH-cytochrome P450 reductase. J. Biol. Chem. 256 (1981) 7478-7486
31. Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S.S., and Kim J.P. Three dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 8411-8416
32. Nadler S.G., and Strobel H.W. Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450. Arch. Biochem. Biophys. 290 (1991) 277-284
33. Shen S., and Strobel H.W. Probing the putative cytochrome P450- and cytochrome c-binding sites on NADPH-cytochrome P450 reductase by anti-peptide antibodies. Biochemistry 33 (1994) 8807-8812
34. Sevrioskova I.F., Li H., Zhang H., Peterson J.A., and Poulos T.L. Structure of cytochrome P450-redox partner electron-transfer complex. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 1863-1868