Yeast cytochrome c peroxidase expression in Escherichia coli and rapid isolation of various highly pure holoenzymes

Protein Expression and Purification

Volumn 19, Issue 1, 2000, Pages 139-147

  Teske, Jennifer G ^a   Savenkova, Marina I ^a   Mauro, J Matthew ^c   Erman, James E ^b   Satterlee, James D ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

^b NORTHERN ILLINOIS UNIVERSITY   (United States)

^c SCIENCE APPLICATIONS INTERNATIONAL CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CHROMATOGRAPHY; CULTURE MEDIUM; CYTOCHOME C PEROXIDASE; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME PURIFICATION; ENZYME SYNTHESIS; ESCHERICHIA COLI; HEMOPROTEIN; RECOMBINANT ENZYME;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034130258     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1220     Document Type: Article

References (37)

1. Everse J., Everse K. E., Grisham M. B. Peroxidases in Chemistry and Biology. 1990;CRC Press, Boca Raton.
2. Poulos T. L. Heme enzyme crystal structures. Adv. Inorg. Biochem. 7:1988;1-36.
3. Bosshard H. R., Anni H., Yonetani T. Yeast cytochrome c peroxidase. Everse J., Everse K. E., Grisham M. B. Peroxidases in Chemistry and Biology. 1990;51-84 CRC Press, Boca Raton.
4. Mauro J. M., Miller M. A., Edwards S. L., Wang J., Fishel L. A., Kraut J. Exploring structure-function relationships in yeast cytochrome c peroxidase using mutagenesis and crystallography. Sigel H., Sigel A. Metal Ions in Biological Systems. 1989;477-503 Dekker, New York.
5. Poulos T. L., Finzel B. C. Heme enzyme structure and function. Protein Peptide Rev. V:1984;115-171.
6. Finzel B. C., Poulos T. L., Kraut J. Crystal structure of yeast cytochrome c peroxidase refined at 1.7Å resolution. J. Biol. Chem. 259:1984;13027-13036.
7. Wang J., Mauro J. M., Edwards S. L., Oatley S. J., Fishel L. A., Ashford V. A., Xuong N., Kraut J. X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis. Biochemistry. 29:1990;7160-7173.
8. Goodin D. B., McRee D. E. The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry. 32:1993;3313-3324.
9. Miller M. A., Geren L., Han G. W., Saunders A., Beasley, Pielak G. J., Durham B., Millett F., Kraut J. Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering. Biochemistry. 35:1996;667-673.
10. B-heme center in terminal oxidases. J. Am. Chem. Soc. 121:1999;8949-8950.
11. Yeung B. K. S., Wang X., Sigman J. A., Petillo P. A., Lu Y. Construction and characterization of a manganese-binding site in cytochrome c peroxidase: Towards a novel manganese peroxidase. Chem. Biol. 4:1997;215-221.
12. Wilcox S. K., Putnam C. D., Sastry M., Blankenship J., Chazin W. J., McRee D. E., Goodin D. B. Rational design of a functional metalloenzyme: Introduction of a site for manganese binding and oxidation Into heme peroxidase. Biochemistry. 37:1998;16853-16862.
13. Fitzgerald M. M., Musah R. A., Rees D. A., Goodin D. B. A ligand-gated hinged loop rearrangement opens a channel to a buried artifical protein cavity. Nature Struct. Biol. 3:1996;626-634.
14. Bonagura C. A., Sundaramoothy M., Pappa H. S., Patterson W. R., Poulos L. An engineered cation site in cytochrome c peroxidase alters the reactivity of the redox active tryptophan. Biochemistry. 35:1996;6107-6115.
15. Fishel L. A., Villafranca J. E., Mauro J. M., Kraut J. Yeast cytochrome c peroxidase: Mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I. Biochemistry. 26:1987;351-360.
16. Nelson C. E., Sitzman E. V., Kang C. H., Margoliash E. Preparation of cytochrome c peroxidase from bakers yeast. Anal. Biochem. 83:1977;622-631.
17. Yonetani T., Ray G. S. Studies on cytochrome c peroxidase. I. Purification and some properties. J. Biol. Chem. 240:1965;4503-4508.
18. Darwish K., Li H., Poulos T. L. Engineering proteins, subcloning and hyperexpressing oxidoreductase genes. Protein Eng. 4:1991;701-708.
19. English A. M., LaBerge M., Walsh M. Rapid procedure for the isolation of cytochrome c peroxidase. Inorg. Chim. Acta. 123:1986;113-116.
20. Goodin D. B., Davidson M. G., Roe J. A., Mauk A. G., Smith M. Amino acid substitutions at Trp-51 of cytochrome c peroxidase: Effects on coordination, species preference for cytochrome c, and electron transfer. Biochemistry. 30:1991;4953-4962.
21. Takio K., Titani K., Ericsson L. H., Yonetani T. Primary structure of yeast cytochrome c peroxidase. Arch. Biochem. Biophys. 203:1980;615-629.
22. Kaput J., Goltz S., Blobel G. Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. J. Biol. Chem. 257:1982;15054-15058.
23. Alam S. L., Satterlee J. D. Using perdeuterated protein to make prosthetic group proton resonance assignments: Glycera dibranchiata monomer hemoglobin component IV as an example. J. Am. Chem. Soc. 117:1995;49-53.
24. Alam S. L., Dutton D. P., Satterlee J. D. Recombinant perdeuterated proteins as an efficient method for making unambiguous heme protein resonance assignments. NATO Adv. Res. Ser. B. 457:1995;123-140.
25. Maniatis T., Fritsch E. F., Sambrook J. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
26. Innis M. A., Gelfand D. H., Sninsky J. J., White T. J. PCR Protocols: A Guide to Methods and Applications. 1990;Academic Press, New York.
27. Rivera M., Walker F. A. Biosynthetic preparation of isotopically labeled heme. Anal. Biochem. 230:1995;295-302.
28. 5. J. Biol. Inorg. Chem. 4:1999;87-98.
29. Vitello L. B, Huang M., Erman J. E. pH-dependent spectral and kinetic properties of cytochrome c peroxidase: Comparison of freshly isolated and stored enzyme. Biochemistry. 29:1990;4283-4288.
30. 2 solutions in the uv). Anal. Biochem. 49:1972;474-478.
31. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976.
32. Neidhardt F. C. Escherichia coli and salmonella. Cellular and Molecular Biology. 1996;ASM Press, Washington. p. 14.
33. 1H nmr study of ferric low-spin cytochrome c peroxidase and horseradish peroxidase. Inorg. Chem. 30:1991;4510-4516.
34. Satterlee J. D., Erman J. E., Mauro J. M., Kraut J. Comparative proton nmr analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an aA235→Asn235 mutant. Biochemistry. 29:1990;8797-8804.
35. Cao, Y, Musah, R. A, Goodin, D. B, and, Mcree, D. E. 1998, Probing the strength and character of an asp-his hydrogen bond by introducing buried charges. Cited as to be published: Protein Data Bank Citation 1A2F.
36. Vitello L. B., Erman J. E., Mauro J. M., Kraut J. Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants. Biochim. Biophy. Acta. 1038:1990;90-97.
37. Satterlee J. D., Erman J. E., LaMar G. N., Smith K. M., Langry K. C. Assignment of hyperfine shifted resonances in high-spin forms of cytochrome c peroxidase by reconstitutions with deuterated hemins. Biochim. Biophys. Acta. 743:1983;246-255.