Role of a highly conserved electrostatic interaction on the surface of cytochrome c in control of the redox function

Biochemistry

Volumn 49, Issue 1, 2010, Pages 42-48

  Tai, Hulin ^a   Mikami, Shin Ichi ^a   Irie, Kiyofumi ^a   Watanabe, Naoki ^a   Shinohara, Naoya ^a   Yamamoto, Yasuhiko ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINO ACID RESIDUES; CYTOCHROME C; DENATURATION TEMPERATURES; ELECTROSTATIC INTERACTIONS; ENTROPIC CONTRIBUTIONS; FUNCTIONAL CONTROL; FUNCTIONAL PROPERTIES; HEME IRON; HYDROGENOBACTER THERMOPHILUS; IN-CONTROL; INTRAMOLECULAR INTERACTIONS; MOLECULAR MECHANISM; NEGATIVE SHIFT; PROTEIN STABILITY; PROTEIN STRUCTURES; REDOX POTENTIALS; STRUCTURAL FEATURE;

AMINO ACIDS; CONTROL SURFACES; ELECTROSTATICS; HEMOGLOBIN; METAL RECOVERY; ORGANIC ACIDS; PORPHYRINS; THERMODYNAMIC PROPERTIES;

ELECTROSTATIC SEPARATORS;

ALANINE; AMINO ACID; CYTOCHROME C; HEME; IRON; LYSINE;

ARTICLE; DENATURATION; ELECTRICITY; ENTROPY; MOLECULAR INTERACTION; MUTATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS;

BACTERIA; BACTERIAL PROTEINS; CIRCULAR DICHROISM; CYTOCHROMES C; MODELS, MOLECULAR; MUTATION; OXIDATION-REDUCTION; PROTEIN CONFORMATION; STATIC ELECTRICITY; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

HYDROGENOBACTER THERMOPHILUS;

EID: 73449136893     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901484b     Document Type: Article

References (42)

1. ms spanning 800 mV. Proteins 75, 719-734.
2. Moore, G. R., and Pettigrew, G. W. (1990) Cytochromes c: Evolutionary, structural, and physicochemical aspects , Springer-Verlag, Berlin.
3. Scott, R. A., and Mauk, A. G., eds. (1996) Cytochrome c: A multidisciplinary approach , University Science Books, Sausalito, CA.
4. Warshel, A., Papazyan, A., and Muegge, I. (1997) Microscopic and semimacroscopic redox calculations: what can and cannot be learned from continuum models. J. Biol. Inorg. Chem. 2, 143-152.
5. Gunner, M. R., Alexov, E., Torres, E., and Lipovaca, S. (1997) The importance of the protein in controlling the electrochemistry of heme metalloproteins: Methods of calculation and analysis. J. Biol. Inorg. Chem. 2, 126-134.
6. Battistuzzi, G., Bellei, M., Borsari, M., Canters, G. W., de Waal, E., Jeuken, L. J., Ronieri, A., and Sola, M. (2003) Control of metalloprotein reduction potential: Compensation phenomena in the reduction thermodynamics of blue copper proteins. Biochemistry 42, 9214-9220.
7. Blouin, C., and Wallace, C. J. A. (2001) Protein matrix and dielectric effect in cytochrome c. J. Biol. Chem. 276, 28814-28818.
8. 562 variants: A library for examining redox potential evolution. Biochemistry 39, 6075-6082.
9. 552 from Hydrogenobacter thermophilus. J. Biol. Chem. 280, 25729-25734.
10. 551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms. J. Mol. Biol. 156, 389-409.
11. 552. J. Biol. Chem. 274, 37533-37537.
12. 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.
13. 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.
14. Yamamoto, Y., Terui, N., Tachiiri, N., Minakawa, K., Matsuo, H., Kameda, T., Hasegawa, J., Sambongi, Y., Uchiyama, S., Kobayashi, Y., and Yamamoto, Y. (2002) Influence of amino acid side chain packing on Fe-methionine coordination in thermostable cytochromes c. J. Am. Chem. Soc. 124, 11574-11575.
15. 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.
16. 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.
17. a of a buried heme propionic acid side-chain. Biochemistry 44, 5488-5494.
18. 551. Biochemistry 48, 8062-8069.
19. Takayama, S. J., Irie, K., Tai, H., Kawahara, T., Hirota, S., Takabe, T., Alcaraz, L. A., Donaire, A., and Yamamoto, Y. (2009) Electron transfer from cytochrome c to cupredoxin. J. Biol. Inorg. Chem. 14, 821-828.
20. van den Burg, B., and Eijsink, V. G. H. (2002) Selection of mutations for increasing protein stability. Curr. Opin. Biotechnol. 13, 333-337.
21. 552. Biochemistry 45, 11005-11011.
22. 551: Role of electrostatic interactions on the hydrophobic collapse and transition state properties. J. Mol. Biol. 289, 1459-1467.
23. Piotte, M., Saudek, V., and Skleńa, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biol. NMR 2, 661-665.
24. 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.
25. 552 relevant to its redox potential. Biochemistry 46, 9215-9224.
26. Yee, E. L., Cave, R. J., Guyer, K. L., Tyma, P. D., and Weaver, M. J. (1979) A survey of ligand effects upon the reaction entropies of some transition metal redox couples. J. Am. Chem. Soc. 101, 1131-1137.
27. 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.
28. 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.
29. Bertini, I., and Luchinat, C. (1986) NMR of paramagnetic molecules in biological systems , pp 19-46, Benjamin/Cummings Publishing Co., Menlo Park, CA.
30. Yamamoto, Y. (1998) NMR study of active sites in paramagnetic hemoproteins. Annu. Rep. NMR Spectrosc. 36, 1-77.
31. Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665.
32. 551. Chem. Lett. 35, 528-529.
33. Komar-Panicucci, S., Weis, D., Bakker, G., Qiao, T., Sherman, F., and McLendon, G. (1994) Thermodynamics of the equilibrium unfolding of oxidized and reduced Saccharomyces cerevisiae Iso-1-cytochromes c. Biochemistry 33, 10556-10560.
34. Battistuzzi, G., Borsari, M., Sola, M., and Francia, F. (1997) Redox thermodynamics of the native and alkaline forms of eukaryotic and bacterial class I cytochromes c. Biochemistry 36, 16247-16258.
35. Tezcan, F. A., Winkler, J. R., and Gray, H. B. (1998) Effects of ligation and folding on reduction potentials of heme proteins. J. Am. Chem. Soc. 120, 13383-13388.
36. Battistuzzi, G., Borsari, M., and Sola, M. (2001) Medium and temperature effects on the redox chemistry of cytochrome c. Eur. J. Inorg. Chem. 2001, 2989-3004.
37. 2+ couple in horseradish peroxidase and its cyanide complex. J. Am. Chem. Soc. 124, 26-27.
38. Rovira, C., Carloni, P., and Parrinello, M. (1999) The iron-sulfur bond in cytochrome c. J. Phys. Chem. B 103, 7031-7035.
39. Battistuzzi, G., Borsari, M., Ronieri, A., and Sola, M. (2004) Solventbased deuterium isotope effects on the redox thermodynamics of cytochrome c. J. Biol. Inorg. Chem. 9, 781-781.
40. 2+ couple in horseradish peroxidase and its cyanide complex. J. Am. Chem. Soc. 124, 26-27.
41. Sola, M, Battistuzzi, G., and Borsari, M. (2005) Modulation of the free energy of reduction in metalloproteins. Chemtracts: Inorg. Chem. 18, 73-86.
42. 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.