- 1) Mao, J., Hauser, K., and Gunner, M. R., How cytochromes with different folds control heme redox potentials. Biochemistry, 42, 9829–9840 (2003).
- 2) Shifman, J. M., Gibney, B. R., Eryl Sharp, R., and Dutton, P. L., Heme redox potential control in de novo designed four-α-helix bundle proteins. Biochemistry, 39, 14813–14821 (2000).
- 3) Hilgen-Willis, S., Bowden, E. F., and Pielak, G. J., Dramatic stabilization of ferricytochrome c upon reduction. J. Inorg. Chem., 51, 649–653 (1993).
- 4) Bertini, I., Cavallaro, G., and Rosato, A., Cytochrome c: occurrence and functions. Chem. Rev., 106, 90–115 (2006).
- 5) Sambongi, Y., Uchiyama, S., Kobayashi, Y., Igarashi, Y., and Hasegawa, J., Cytochrome c from a thermophilic bacterium has provided insights into the mechanism of protein maturation, folding, and stability. Eur. J. Biochem., 269, 3355–3361 (2002).
- 6) Nakamura, S., Ichiki, S., Takashima, H., Uchiyama, S., Hasegawa, J., Kobayashi, Y., Sambongi, Y., and Ohkubo, T., Structure of cytochrome c 552 from a moderate thermophilic bacterium, Hydrogenophilus thermoluteolus: comparative study on the thermostability of cytochrome c. Biochemistry, 45, 6115–6123 (2006).
- 7) Uchiyama, S., Ohshima, A., Nakamura, S., Hasegawa, J., Terui, N., Takayama, S. J., Yamamoto, Y., Sambongi, Y., and Kobayashi, Y., Complete thermal-unfolding profiles of oxidized and reduced cytochromes c. J. Am. Chem. Soc., 126, 14684–14685 (2004).
- 8) Takahashi, Y., Sasaki, H., Takayama, S. J., Mikami, S., Kawano, S., Mita, H., Sambongi, Y., and Yamamoto, Y., Further enhancement of the thermostability of Hydrogenobacter thermophilus cytochrome c 552. Biochemistry, 45, 11005–11011 (2006).
- 9) Hasegawa, J., Shimahara, H., Mizutani, M., Uchiyama, S., Arai, H., Ishii, M., Kobayashi, Y., Ferguson, S. J., Sambongi, Y., and Igarashi, Y., Stabilization of Pseudomonas aeruginosa cytochrome c 551 by systematic amino acid substitutions based on the structure of thermophilic Hydrogenobacter thermophilus cytochrome c 552. J. Biol. Chem., 274, 37533–37537 (1999).
- 10) Oikawa, K., Nakamura, S., Sonoyama, T., Ohshima, A., Kobayashi, Y., Takayama, S. J., Yamamoto, Y., Uchiyama, S., Hasegawa, J., and Sambongi, Y., Five amino acid residues responsible for the high stability of Hydrogenobacter thermophilus cytochrome c 552: reciprocal mutation analysis. J. Biol. Chem., 280, 5527–5532 (2005).
- 11) Pace, C. N., and Shaw, K. L., Linear extrapolation method of analyzing solvent denaturation curves. Proteins, Suppl. 4, 1–7 (2000).
- 12) Terui, N., Tachiiri, N., Matsuo, H., Hasegawa, J., Uchiyama, S., Kobayashi, Y., Igarashi, Y., Sambongi, Y., and Yamamoto, Y., Relationship between redox function and protein stability of cytochromes c. J. Am. Chem. Soc., 125, 13650–13651 (2003).
- 13) Mason, P. E., Neilson, G. W., Dempsey, C. E., Barnes, A. C., and Cruickshank, J. M., The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solution. Proc. Natl. Acad. Sci. USA, 100, 4557–4561 (2003).
- 14) Hakamada, S., Sonoyama, T., Ichiki, S., Nakamura, S., Uchiyama, S., Kobayashi, Y., and Sambongi, Y., Stabilization mechanism of cytochrome c 552 from a moderately thermophilic bacterium, Hydrogenophilus thermoluteolus. Biosci. Biotechnol. Biochem., 72, 2103–2109 (2008).
- 15) Tomlinson, E. J., and Ferguson, S. J., Conversion of a c type cytochrome to a b type that spontaneously forms in vitro from apo protein and heme: implications for c type cytochrome biogenesis and folding. Proc. Natl. Acad. Sci. USA, 97, 5156–5160 (2000).
- 16) Wittung-Stafshede, P., Effect of redox state on unfolding energetics of heme proteins. Biochim. Biophys. Acta, 1432, 401–405 (1999).
- 17) Fisher, M. T., Differences in thermal stability between reduced and oxidized cytochrome b 562 from Escherichia coli. Biochemistry, 30, 10012–10018 (1991).
- 18) Reincke, B., Perez, C., Pristovsek, P., Lucke, C., Ludwig, C., Lohr, F., Rogov, V. V., Ludwig, B., and Ruterjans, H., Solution structure and dynamics of the functional domain of Paracoccus denitrificans cytochrome c 552 in both redox states. Biochemistry, 40, 12312–12320 (2001).
- 19) Voet, D., and Voet, J. G., “Biochemistry 3rd Edition,” Wiley, pp. 803–804 (1990).
- 20) Ogawa, K., Sonoyama, T., Takeda, T., Ichiki, S., Nakamura, S., Kobayashi, Y., Uchiyama, S., Nakasone, K., Takayama, S. J., Mita, H., Yamamoto, Y., and Sambongi, Y., Roles of a short connecting disulfide bond in the stability and function of psychrophilic Shewanella violacea cytochrome c 5. Extremophiles, 11, 797–807 (2007).
Full access
Correlation between the Stability and Redox Potential of Three Homologous Cytochromes c from Two Thermophiles and One Mesophile
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.