Enhancement of the thermostability of hydrogenobacter thermophilus cytochrome c 552 through introduction of an extra methylene group into its hydrophobic protein interior

Biochemistry

Volumn 50, Issue 15, 2011, Pages 3161-3169

  Tai, Hulin ^a   Irie, Kiyofumi ^a   Mikami, Shin Ichi ^a   Yamamoto, Yasuhiko ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; DENATURATION TEMPERATURES; DIFFERENT EFFECTS; FUNCTIONAL CONTROL; FUNCTIONAL PROPERTIES; HYDROGENOBACTER THERMOPHILUS; HYDROPHOBIC CORE; HYDROPHOBIC PROTEIN; HYDROPHOBIC RESIDUES; METHYL GROUP; METHYLENE GROUPS; NEGATIVE SHIFT; PROTEIN ENGINEERING; REDOX FORMS; REDOX POTENTIALS; VOID SPACE; WILD-TYPE PROTEINS; X-RAY STRUCTURE;

FUNCTIONAL GROUPS; GENETIC ENGINEERING; HYDROPHOBICITY; PORPHYRINS; REDOX REACTIONS;

PROTEINS;

BACTERIAL PROTEIN; CARBENE; CYTOCHROME; CYTOCHROME C552; LEUCINE; MUTANT PROTEIN; UNCLASSIFIED DRUG; VALINE;

ARTICLE; CONTROLLED STUDY; ENTHALPY; HYDROGENOBACTER THERMOPHILUS; HYDROPHOBICITY; MUTATION; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STABILITY; PROTEIN STRUCTURE; STEREOCHEMISTRY; TEMPERATURE DEPENDENCE; THERMOPHILIC BACTERIUM; THERMOSTABILITY; WILD TYPE; X RAY ANALYSIS;

AMINO ACID SUBSTITUTION; AQUIFOLIACEAE; CATALYTIC DOMAIN; CYTOCHROME C GROUP; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MUTATION; PROTEIN ENGINEERING; TEMPERATURE; TRANSITION TEMPERATURE;

HYDROGENOBACTER THERMOPHILUS;

EID: 79953883486     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200256d     Document Type: Article

References (35)

1. Vinther, J. M., Kristensen, S. M., and Led, J. J. (2010) Enhanced stability of a protein with increasing temperature J. Am. Chem. Soc. 133, 271-278
2. Atomi, H. (2005) Recent progress toward the application of hyperthermophiles and their enzymes Curr. Opin. Chem. Biol. 9, 166-173 (Pubitemid 40462486)
3. Cambillau, C. and Claverie, J. (2000) Structural and genomic correlates of hyperthermostability J. Biol. Chem. 275, 32383-32386 and references therein
4. 1H-NMR spectroscopy Biochemistry 37, 9641-9649 (Pubitemid 28319608)
5. 552 J. Biol. Chem. 274, 37533-37537 (Pubitemid 30026806)
6. Hasegawa, J., Uchiyama, S., Tanimoto, Y., Mizutani, M., Kobayashi, Y., Sambongi, Y., and Igarashi, Y. (2000) Selected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpart J. Biol. Chem. 275, 37824-37828 (Pubitemid 32004899)
7. Uchiyama, S., Hasegawa, J., Tanimoto, Y., Moriguchi, H., Mizutani, M., Igarashi, Y., Sambongi, Y., and Kobayashi, Y. (2002) Thermodynamic characterization of variants of mesophilic cytochrome c and its thermophilic counterpart Protein Eng. 15, 455-461 (Pubitemid 34742252)
8. Sambongi, Y., Uchiyama, S., Kobayashi, Y., Igarashi, Y., and Hasegawa, J. (2002) Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability Eur. J. Biochem. 269, 3355-3361 (Pubitemid 34988977)
9. Yamamoto, Y., Terui, N., Tachiiri, N., Minakawa, K., Matsuo, H., Kameda, T., Hasegawa, J., Sambongi, Y., Uchiyama, S., Kobayashi, Y., and Igarashi, Y. (2002) Influence of amino acid side chain packing on Fe-methionine coordination in thermostable cytochrome c J. Am. Chem. Soc. 124, 11574-11575
10. Terui, N., Tachiiri, N., Matsuo, H., Hasegawa, J., Uchiyama, S., Kobayashi, Y., Igarashi, Y., Sambongi, Y., and Yamamoto, Y. (2003) Relationship between redox function and protein stability of cytochromes c J. Am. Chem. Soc. 125, 13650-13651 (Pubitemid 37386025)
11. Uchiyama, S., Ohshima, A., Nakamura, S., Hasegawa, J., Terui, N., Takayama, S. J., Yamamoto, Y., Sambongi, Y., and Kobayashi, Y. (2004) Complete thermal-unfolding profiles of oxidized and reduced cytochromes c J. Am. Chem. Soc. 126, 14684-14685 (Pubitemid 39532127)
12. a of a buried heme propionic acid side chain Biochemistry 44, 5488-5494 (Pubitemid 40489988)
13. 552 J. Biol. Chem. 280, 5527-5532 (Pubitemid 40280030)
14. Sanbongi, Y., Ishii, M., Igarashi, Y., and Kodama, T. (1989) Amino acid sequence of cytochrome c-552 from a thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus J. Bacteriol. 171, 65-69
15. 551 Chem. Lett. 35, 528-529 (Pubitemid 44154245)
16. 552 from Hydrogenobacter thermophilus J. Biol. Chem. 280, 25729-25734 (Pubitemid 40962282)
17. 551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms J. Mol. Biol. 156, 389-409 (Pubitemid 12116318)
18. 552 Biochemistry 45, 11005-11011 (Pubitemid 44360171)
19. Lojou, E. and Bianco, P. (2000) Membrane electrodes can modulate the electrochemical response of redox potentials - Direct electrochemistry of cytochrome c J. Electroanal. Chem. 485, 71-80
20. 552 relevant to its redox potential Biochemistry 46, 9215-9224 (Pubitemid 47255036)
21. Battistuzzi, G., Borsari, M., Loschi, L., Menziani, M. C., De Rienzo, F., and Sola, M. (2001) Control of metalloprotein reduction potential: The role of electrostatic and solvation effects probed on plastocyanin mutants Biochemistry 40, 6422-6430 (Pubitemid 32472732)
22. Piotte, M., Saudek, V., and Sklená, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J. Biol. NMR 2, 661-665
23. La Mar, G. N., Satterlee, J. D., and de Ropp, J. S. (2000) Nuclear magnetic resonance of hemoproteins, in The Porphyrin Handbook (Kadish, K., Smith, K. M., and Guilard, R., Eds.) pp 185 - 298, Academic Press, New York.
24. Bertini, I. and Luchinat, C. (1986) NMR of Paramagnetic Molecules in Biological Systems, pp 19 - 46, The Benjamin/Cummings Publishing Company, Menlo Park, CA.
25. Yamamoto, Y. (1998) NMR study of active sites in paramagnetic hemoproteins Ann. Rep. NMR Spectrosc. 36, 1-77
26. Tai, H., Mikami, S., Irie, K., Watanabe, N., Shinohara, N., and Yamamoto, Y. (2010) Role of a highly conserved electrostatic interaction on the surface of cytochrome c in control of the redox function Biochemistry 49, 42-48
27. 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 (Pubitemid 39294699)
28. 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 (Pubitemid 28562297)
29. 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 (Pubitemid 28089895)
30. La Mar, G. N. (1973) NMR of Paramagnetic Molecules (La Mar, G. N., Horrocks, W. D., Jr., and Holm, R. H., Eds.) pp 86 - 126, Academic Press, New York.
31. 551 Biochemistry 49, 42-48
32. 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 (Pubitemid 29113809)
33. Battistuzzi, G., Borsari, M., Ronieri, A., and Sola, M. (2004) Solvent-based deuterium isotope effects on the redox thermodynamics of cytochrome c J. Biol. Inorg. Chem. 9, 781-781
34. 2+ couple in horseradish peroxidase and its cyanide complex J. Am. Chem. Soc. 124, 26-27 (Pubitemid 34037544)
35. Sola, M, Battistuzzi, G., and Borsari, M. (2005) Modulation of the free energy of reduction in metalloproteins Chemtracts-Inorg. Chem. 18, 73-86 (Pubitemid 41805866)