Suppression of axial methionine fluxion in Hydrogenobacter thermophilus Gln64Asn cytochrome c552

Biochemistry

Volumn 44, Issue 13, 2005, Pages 5225-5233

  Wen, Xin ^a   Bren, Kara L ^a  

^a UNIVERSITY OF ROCHESTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRONIC STRUCTURE; MOLECULAR ORIENTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

AXIAL MET ORIENTATION; CYTOCHROME C; METHIONINE FLUXION; PERIPHERAL INTERACTIONS;

BACTERIA;

CYTOCHROME C; CYTOCHROME C552; METHIONINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; ENZYME CONFORMATION; ENZYME STRUCTURE; HYDROGENOBACTER THERMOPHILUS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; PSEUDOMONAS AERUGINOSA; STRUCTURE ANALYSIS; WILD TYPE;

AMINO ACID SUBSTITUTION; BACTERIA; BASE SEQUENCE; CYTOCHROME C GROUP; DNA, BACTERIAL; ELECTROCHEMISTRY; GENES, BACTERIAL; HEME; METHIONINE; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

HYDROGENOBACTER THERMOPHILUS; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 16444374800     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047556+     Document Type: Article

References (49)

1. Que, L., and Tolman, W. B. (2004) Recurring structural motifs in bioinorganic chemistry, in Comprehensive Coordination Chemistry II (McCleverty, J. A., and Meyer, T. J., Eds.) Vol. 8, pp 1-15, Elsevier, Berlin.
2. Winkler, J. R., Wittung-Stafshede, P., Leckner, J., Malmström, B. G., and Gray, H. B. (1997) Effects of folding on metalloprotein active sites, Proc. Natl. Acad. Sci. U.S.A. 94, 4246-4249.
3. Cotton, F. A., Wilkinson, G., Murillo, C. A., and Bochmann, M. (1999) Advanced Inorganic Chemistry, 6th ed., pp 13-24, Wiley, New York.
4. Toyota, S. (1999) Mechanisms of inversion at pyramidal sulfur atoms in three-coordinate sulfur compounds, Rev. Heteroat. Chem. 21, 139-162.
5. 552, Proc. Natl. Acad. Sci. U.S.A. 101, 8637-8642.
6. Bren, K. L., Kellogg, J. A., Kaur, R., and Wen, X. (2004) Folding, conformational changes, and dynamics of cytochromes c probed by NMR spectroscopy, Inorg. Chem. 43, 12162-12176.
7. Scott, R. A., and Mauk, A. G. (1996) Cytochrome c: A Multidisciplinary Approach, University Science Books, Sausalito, CA.
8. Moore, G. R., and Pettigrew, G. W. (1990) Cytochrome c: Evolutionary, Structural and Physicochemical Aspects, Springer-Verlag, New York.
9. Lee, K.-B., La Mar, G. N., Mansfield, K. E., Smith, K. M., Pochapsky, T. C., and Sligar, S. G. (1993) Interpretation of hyperfine shift patterns in ferricytochrome b(5) in terms of angular position of the heme-a sensitive probe for peripheral heme protein interactions, Biochim. Biophys. Acta 1202, 189-199.
10. LaMar, G. N., Satterlee, J. D., and deRopp, J. S. (2000) Nuclear magnetic resonance of hemoproteins, in The Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Ruilard, R., Eds.) Vol. 5, pp 185-298, Academic Press, New York.
11. Kurland, R. J., and McGarvey, B. R. (1970) Isotropic NMR shifts in transition metal complexes: The calculation of the Fermi contact and pseudocontact terms, J. Magn. Reson. 2, 286-301.
12. Bertini, I., and Luchinat, C. (1996) NMR of paramagnetic substances, Coord. Chem. Rev. 150, 29-75.
13. Shokhirev, N. V., and Walker, F. A. (1998) The effect of axial ligand plane orientation on the contact and pseudocontact shifts of low-spin ferriheme proteins, J. Biol. Inorg. Chem. 3, 581-594.
14. Senn, H., and Wüthrich, K. (1985) Amino acid sequence, heme-iron coordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes, Q. Rev. Biophys. 18, 111-134.
15. Senn, H., Keller, R. M., and Wüthrich, K. (1980) Difference in the chirality of the axial methionine in homologous cytochromes c determined by H-1-NMR and CD spectroscopy, Biochem. Biophys. Res. Commun. 92, 1362-1369.
16. Karan, E. F., Russell, B. S., and Bren, K. L. (2002) Characterization of Hydrogenobacter thermophilus cytochromes c(552) expressed in the cytoplasm and periplasm of Escherichia coli, J. Biol. Inorg. Chem. 7, 260-272.
17. Timkovich, R., Cai, M., Zhang, B., Arciero, D. M., and Hooper, A. B. (1994) Characteristics of the paramagnetic H-1-NMR spectra of the ferricytochrome c-551 family, Eur. J. Biochem. 226, 159-168.
18. Shokhirev, N. V., and Walker, F. A. (1998) Co- and counterrotation of magnetic axes and axial ligands in low-spin ferriheme systems, J. Am. Chem. Soc. 120, 981-990.
19. Turner, D. L. (1995) Determination of heme electronic structure in His-Met cytochromes c by C-13 NMR-The effect of the axial ligands, Eur. J. Biochem. 227, 829-837.
20. 1H NMR spectroscopy, Biochemistry 37, 9641-9649.
21. Timkovich, R., Bergmann, D., Arciero, D. M., and Hooper, A. B. (1998) Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea, Biophys. J. 75, 1964-1972.
22. Matsuura, Y., Takano, T., and Dickerson, R. E. (1982) Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the 2 redox forms, J. Mol Biol. 156, 389-409.
23. Sambrook, J., Fritsch, E. F., and Manaiatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, New York.
24. Arslan, E., Schulz, H., Zufferey, R., Künzler, P., and Thöny-Meyer, L. (1998) Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb(3) oxidase in Escherichia coli, Biochem. Biophys. Res. Commun. 251, 744-747.
25. 551, J. Biol. Inorg. Chem. 8, 156-166.
26. Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
27. Wüthrich, K. (1986) NMK of Proteins and Nucleic Acids, Wiley, New York.
28. Scheijter, A. (1996) Oxidation state-dependent properties of cytochromes c, in Cytochrome c: A Multidisciplinary Approach (Scott, R. A., and Mauk, A. G., Eds.) pp 335-345, University Science Books, Mill Valley, CA.
29. Berghuis, A. M., and Brayer, G. D. (1992) Oxidation state-dependent conformational changes in cytochrome c, J. Mol. Biol. 223, 959-976.
30. Emerson, S. D., and La Mar, G. N. (1990) NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: A new probe of steric tilt of bound ligand, Biochemistry 29, 1556-1566.
31. Horio, T., Higashi, T., Sasagawa, M., Kusai, K., Nakai, M., and Okunuki, K. (1960) Preparation of crystalline Pseudomonas cytochrome c-551 and its general properties, Biochem. J. 77, 194-201.
32. Margoliash, E., and Frohwirt, N. (1959) Spectrum of horse heart cytochrome c, Biochem. J. 71, 570-572.
33. Harbury, H. A., Cronin, J. R., Fanger, M. W., Hettinger, T. P., Murphy, A. J., Myer, Y. P., and Vinogradov, S. N. (1965) Complex formation between methionine and a heme peptide from cytochrome c, Proc. Natl. Acad. Sci. U.S.A. 54, 1658-1664.
34. Kohler, M., Gafert, J., Friedrich, J., Vanderkooi, J. M., and Laberge, M. (1996) Stark effect experiments in cytochrome c-type proteins: Structural hierarchies, Biophys. J. 71, 77-85.
35. Fee, J. A., Chen, Y., Todaro, T. R., Bren, K. L., Patel, K. M., Hill, M. G., Gomez-Moran, E., Loehr, T. M., Ai, J., Thöny-Meyer, L., Williams, P. A., Stura, E., Sridhar, V., and McRee, D. E. (2000) Integrity of Thermus thermophilus cytochrome c(552) synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH. Biochemical, spectral, and structural characterization of the recombinant protein, Protein Sci. 9, 2074-2084.
36. Timkovich, R., and Cai, M. L. (1993) Investigation of the structure of oxidized Pseudomonas aeruginosa cytochrome c551 by NMR-Comparison of observed paramagnetic shifts and calculated pseudocontact shifts, Biochemistry 32, 11516-11523.
37. Low, D. W., Gray, H. B., and Duus, J. Ø. (1997) Paramagnetic NMR spectroscopy of microperoxidase-8, J. Am. Chem. Soc. 119, 1-5.
38. Mondelli, R., Scaglioni, L., Mazzini, S., Bolis, G., and Ranghino, G. (2000) 3D structure of microperoxidase-11 by NMR and molecular dynamic studies, Magn. Reson. Chem. 38, 229-240.
39. Tachiiri, N., Hemmi, H., Takayama, S. J., Mita, H., Hasegawa, J., Sambongi, Y., and Yamamoto, Y. (2004) Effects of axial methionine coordination on the in-plane asymmetry of the heme electronic structure of cytochrome c, J. Biol. Inorg. Chem. 9, 733-742.
40. Banci, L., Bertini, I., Huber, J. G., Spyroulias, G. A., and Turano, P. (1999) Solution structure of reduced horse heart cytochrome c, J. Biol. Inorg. Chem. 4, 21-31.
41. Baistrocchi, P., Banci, L., Bertini, I., Turano, P., Bren, K. L., and Gray, H. B. (1996) Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c, Biochemistry 35, 13788-13696.
42. Chau, M.-H., Cai, M. L., and Timkovich. R. (1990) NMR comparison of prokaryotic and eukaryotic cytochromes c, Biochemistry 29, 5076-5087.
43. Tresoldi, G., Lo Schiavo, S., Lanza, S., and Cardiano, P. (2002) A congested Ru(dps)(2) or Ru(dprs)(2) core (dps = di-2-pyridyl Sulfide; dprs = di-2-pyrimidinyl sulfide) promotes sulfur inversion of N,S-chelate thioethers containing CH2R and 2-pyridyl or 2-pyrimidinyl groups, Eur. J. Inorg. Chem. 1, 181-191.
44. Pollock, W. B. R., Rosell, F. I., Twitchett, M. B., Dumont, M. E., Mauk, A. G. (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition, Biochemistry 37, 6124-6131.
45. Kellogg, J. A., and Bren, K. L. (2002) Characterization of recombinant horse cytochrome c synthesized with the assistance of Escherichia coli cytochrome c maturation factors, Biochim. Biophys. Acta 1601, 215-221.
46. Berghuis, A. M., Guillemette, J. G., Smith, M., and Brayer, G. D. (1994) Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment, J. Mol. Biol. 235, 1326-1341.
47. Lett, C. M., and Guillemette, J. G. (2002) Increasing the redox potential of isoform 1 of yeast cytochrome c through the modification of select haem interactions, Biochem. J. 362, 281-287.
48. Stuchebrukhov, A. A., and Marcus, R. A. (1995) Theoretical study of electron transfer in ferrocytochromes, J. Phys. Chem. 99, 7581-7590.
49. Detlefsen, D. J., Thanabal, V., Pecoraro, V. L., and Wagner, G. (1990) Sequential proton NMR assignments of iron(II) cytochrome-c551 from Pseudomonas aeruginosa, Biochemistry 29, 9377-9386.