Conversion of the Escherichia coli cytochrome b562 to an archetype cytochrome b: A mutant with bis-histidine ligation of heme iron

Biochemistry

Volumn 44, Issue 1, 2005, Pages 431-439

  Hay, Sam ^a   Wydrzynski, Tom ^a  

^a AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

MUTAGENESIS; PARAMAGNETIC RESONANCE; PH EFFECTS; PROTEINS; SOLVENTS;

CHEMICAL STABILITY; CYTOCHROMES; HISTIDINE; MIDPOINT POTENTIAL;

ESCHERICHIA COLI;

ASPARAGINE; CYTOCHROME B; CYTOCHROME B562; HEME; HISTIDINE; METHIONINE; MUTANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; MOLECULAR MODEL; OXIDATION REDUCTION POTENTIAL; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; THERMOSTABILITY; WILD TYPE;

BASE SEQUENCE; CLONING, MOLECULAR; CYTOCHROME B GROUP; DNA PRIMERS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEME; IRON; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 11844263892     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0492298     Document Type: Article

References (47)

1. 562, I. J. Biol. Chem. 241, 3687-3695.
2. Rotsaert, F. A. J., Hallberg, B. M., de Vries, S., Moenne-Loccoz, P., Divne, C., Renganathan, V., and Gold, M. H. (2003) Biophysical and structural analysis of a novel heme b iron ligation in the flavocytochrome cellobiose dehydrogenase, J. Biol. Chem. 278, 33224-33231.
3. 562 from Escherichia coli at 1.4 Å resolution, J. Mol. Biol. 247, 947-962.
4. 562, Biochemistry 38, 8657-8670.
5. 562, Biochim. Biophys. Acta 829, 83-96.
6. 562. 1. Spectroscopic and electrochemical characterization of the electronic properties, Biochemistry 35, 13618-13626.
7. 562, Biochemistry 36, 16141-16146.
8. 562 redox variants: Evolutionary strategies for modulating redox potential revealed using a library approach, Biochemistry 41, 4321-4328.
9. Razeghifard, M. R., and Wydrzynski, T. (2003) Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation, Biochemistry 42, 1024-1034.
10. Teale, F. W. F. (1959) Cleavage of haem - protein link by acid methylethyl ketone, J. Biochim. Biophys. Acta 35, 543.
11. Gibney, B. R., and Dutton, P. L. (2001) De novo design and synthesis of heme proteins, in Advances in Inorganic Chemistry (Mauk, A. G, and Sykes, A. G., Eds.) Vol. 51, pp 409-455, Academic Press, New York.
12. Lombardi, A., Nastri, F., Pavone, V. (2001) Peptide-based heme - protein models, Chem. Rev. 101, 3165-3189
13. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 131, 266-280.
14. 562. Protein Sci. 7, 961-965.
15. Dutton, P. L. (1978) Redox potentiometry: Determination of midpoint potentials of oxidation - reduction components of biological electron-transfer systems, Methods Enzymol. 54, 411-435.
16. 562 folding triggered by electron transfer, J. Am. Chem. Soc. 119, 9562-9563.
17. Walker, F. A., Huynh, B. H., Scheidt, W. B., and Osvath, S. R. (1986) Models for cytochromes b. Effect of axial ligand plane orientation on the EPR and Mössbauer spectra of low-spin ferrihemes, J. Am. Chem. Soc. 108, 5288-5297.
18. Taylor, C. P. S. (1977) The EPR of low spin heme complexes, Biochim. Biophys. Acta 491, 137-149.
19. Eaton, W. A., and Hochstrasser, R. M. (1967) Electronic spectrum of single crystals of ferricytochrome-c, J. Phys. Chem. 46, 2533-2539.
20. 562, Biochemistry 30, 10150-10155.
21. Zhou, N. E., Kay, C. M., and Hodges, R. S. (1992) Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils, J. Biol. Chem. 267, 2664-2670.
22. 562 from Escherichia coli, Biochemistry 17, 3084-3091
23. Shifman, J. M., Gibney, B. R., Sharp, R. E., and Dutton, P. L. (2000) Heme redox potential control in de novo designed four-α-helix bundle proteins, Biochemistry 39, 14813-14821.
24. Clarke, W. M. (1960) Oxidation - Reduction Potentials of Organic Systems, Bailliere, Tindall, and Cox, Ltd., London, U.K.
25. Huffman, D. L., and Suslick, K. S. (2000) Hydrophobic interactions in metalloporphyrin - peptide complexes, Inorg. Chem. 39, 5418-5419.
26. Nesset, M. J. M., Shokhirev, N. V., Enemark, P. D., Jacobson, S. E., and Walker, F. A. (1996) Models of the cytochromes. Redox properties and thermodynamic stabilities of complexes of hindered iron(III) and iron(II) tetraphenylporphyrinates with substituted pyridines and imidazoles, Inorg. Chem. 35, 5188-5200.
27. 562? Protein Eng. 14, 415-419.
28. 562, J. Am. Chem. Soc. 123, 512-513.
29. 5, Biochemistry 40, 9469-9483.
30. Chothia, C. (1974) Hydrophobic bonding and accessible surface area in proteins, Nature 248, 338-339.
31. Mines, G. A., Pascher, T., Lee, S. C., Winkler, J. R., and Gray, H. B. (1996) Cytochrome c folding triggered by electron transfer, Chem. Biol. 3, 491-497.
32. Bixler, J., Bakker, G., and McLendon, G. (1992) Electrochemical probes of protein folding, J. Am. Chem. Soc. 114, 6938-6939.
33. Meyer, T. E., and Kamen, M. D. (1982) New perspectives on c-type cytochromes, Adv. Protein Chem. 35, 105-212.
34. Miller, G. T., Zhang, B., Hardman, J. K., and Timkovich, R. (2000) Converting a c-type to a b-type cytochrome: Met61 to His61 mutant of Pseudomonas cytochrome c551, Biochemistry 39, 9010-9017.
35. 0.0) absorption band of ferrous cytochrome c and other heme proteins, Biochemistry 35, 12820-12830.
36. Othman, S., Le Lirzin, A., and Desbois, A. (1994) Resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: Characterization of the bis(histidine) axial ligation in c-type cytochromes, Biochemistry 33, 15437-15448.
37. Othman, S., and Desbois, A. (1998) Resonance Raman investigation of lysine and n-acetylmethionine complexes of ferric and ferrous microperoxidase, Eur. Biophys. J. 28, 12-25.
38. Romberg, R. W., and Kassner, R. J. (1982) Effects of solvent on the absorption maxima of five-coordinate heme complexes and carbon monoxide-heme complexes as models for the differential spectral properties of hemoglobins and myoglobins, Biochemistry 21, 880-886.
39. Peisach, J., Blumberg, W. E., and Adler, A. (1973) Electron paramagnetic resonance studies of iron porphyrin and chlorin systems, Ann. N.Y. Acad. Sci. 206, 310-327.
40. Harbury, H. A., and Loach, P. A. (1960) Oxidation-linked proton functions in heme octa- and undecapeptides from mammalian cytochrome c, J. Biol. Chem. 235, 3640-3645.
41. Moore, G. R., and Pettigrew, G. W., Eds. (1990) Cytochromes c. Evolutionary, Structural, and Physicochemical Aspects, Springer-Verlag, Berlin, Germany.
42. 554 from Nitrosomonas europaea, J. Am. Chem. Soc. 125, 1738-1747.
43. Gibney, B. R., Huang, S. S., Skalicky, J. J., Fuentes, E. J., Wand, A. J., and Dutton, P. L. (2001) Hydrophobic modulation of heme properties in heme protein maquettes, Biochemistry 40, 10550-10561.
44. Kennedy, M. L., Silchenko, S., Houndonougbo, N., Gibney, B. R., Dutton, P. L., Rodgers, K. R., and Benson, D. R. (2001) Model hemoprotein reduction potentials: The effects of histidine-to-iron coordination equilibrium, J. Am. Chem. Soc. 123, 4635-4636.
45. 562 variants: A library for examining redox potential evolution, Biochemistry 39, 6075-6082.
46. 562, Inorg. Chim. Acta 252, 71-77.
47. John, D. M., and Weeks, K. M. (2000) van't Hoff enthalpies without baselines, Protein Sci. 9, 1416-1419.