Serine92 (F7) Contributes to the Control of Heme Reactivity and Stability in Myoglobin

Biochemistry

Volumn 32, Issue 19, 1993, Pages 5132-5138

  Smerdon, Stephen J ^a,b   Krzywda, Szymon ^a   Wilkinson, Anthony J ^a   Brantley, Robert E ^c   Carver, Theodore E ^c,d   Hargrove, Mark S ^c   Olson, John S ^c  

^a UNIVERSITY OF YORK   (United Kingdom)

^b YALE UNIVERSITY   (United States)

^c RICE UNIVERSITY   (United States)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; LEUCINE; MYOGLOBIN; SERINE; HEME; HEMIN; HYBRID PROTEIN;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; DISSOCIATION; HYDROGEN BOND; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; SWINE; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; DRUG STABILITY; ESCHERICHIA COLI; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; SITE DIRECTED MUTAGENESIS; X RAY DIFFRACTION;

SUS SCROFA;

AMINO ACID SEQUENCE; ANIMAL; CRYSTALLIZATION; DRUG STABILITY; ESCHERICHIA COLI; HEME; HEMIN; HYDROGEN BONDING; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MYOGLOBIN; RECOMBINANT FUSION PROTEINS; SERINE; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; SWINE; X-RAY DIFFRACTION;

EID: 0027336762     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00070a023     Document Type: Article

References (28)

1. Carver, T. E., Rohlfs, R. J., Olson, J. S., Gibson, Q. H., Blackmore, R. S., Springer, B. A., Egeberg, K. D., & Sligar, S. G. (1990) J. Biol. Chem. 265, 20007–20020.
2. Carver, T. E., Olson, J. S., Smerdon, S. J., Krzywda, S., Wilkinson, A. J., Gibson, Q. H., Blackmore, R. S., Ropp, J. D., & Sligar, S. G. (1991) Biochemistry 30, 4697–4705.
3. Carver, T. E., Brantley, R. E., Singleton, E. W., Arduini, R. M., Quillin, M. L., Phillips, G. N., & Olson, J. S. (1992) J. Biol. Chem. 267, 14443–14450.
4. Dodson, G. G., Hubbard, R. E., Oldfield, T. J., Smerdon, S. J., & Wilkinson, A. J. (1988) Protein Eng. 2, 233–237.
5. Egeberg, K. D., Springer, B. A., Martinis, S. A., Sligar, S. G., Morikis, D., & Champion, P. M. (1990) Biochemistry 29, 9783-9721.
6. Evans, S. V., & Brayer, G. D. (1990) J. Mol. Biol. 213, 885–897.
7. Giacometti, G. M., Ascenzi, P., Bolognesi, M, & Brunori, M. (1981a) J. Mol. Biol. 146, 363–374.
8. Giacometti, G. M., Ascenzi, P., Brunori, M., Rigatti, G., Giacometti, G., & Bolognesi, M. (1981b) J. Mol. Biol. 151, 315–319.
9. Gibson, Q. H., Wittenberg, J. B., Wittenberg, B. A., Bogusz, D., & Appleby, C. A. (1989) J. Biol. Chem. 264, 100–107.
10. Hendrickson, W. A. & Konnert, J. H. (1979) in Biomolecular Structure, Conformation, Function and Evolution (Srinivasan, R., Ed.) Vol 1, pp 43–57, Pergamon, New York.
11. Kabsch, W. (1988) J. Appl. Crystallogr. 21, 916–924.
12. Liddington, R., Derewenda, Z., Dodson, G., & Harris, D. (1988) Nature 331, 725–728.
13. Matsudaira, P. (1987) J. Biol. Chem. 262, 10035–10038.
14. Mathews, A. J., Rohlfs, R. J., Olson, J. S., Tame, J., Renaud, J.-P., & Nagai, K. (1989) J. Biol. Chem. 264, 16573-16383.
15. Mathews, A. J., Olson, J. S., Renaud, J.-P., Tame J., & Nagai, K. (1991) J. Biol. Chem. 266, 21631–21639.
16. Mims, M. P., Porras, A. G., Olson, J. S., Noble, R. W., & Peterson, J. A. (1983) J. Biol. Chem. 258, 14219–14232.
17. Nagai, K., Luisi, B., Shih, K., Miyazaki, G., Imai, K., Poyart, C., De Young, A., Kuriatkowsky, L., Noble, R. W., Lin, S.-H., & Yu, N. T. (1987) Nature 329, 858–860.
18. Oldfield, T. J., Smerdon, S. J., Dauter, Z., Petratos, K., Wilson, K. S., & Wilkinson, A. J. (1992) Biochemistry 31, 8732–8739.
19. Olson, J. S., McKinnie, R. E., Mims, M. P., & White, D. K. (1983) Biochemistry 105, 1522–1527.
20. Olson, J. S., Mathews, A. J., Rohlfs, R. J., Springer, B. A., Egeberg, K., Sligar, S. G., Tame, J., Renaud, J.-P., & Nagai, K. (1988) Nature 336, 265–266.
21. Perutz, M. F. (1970) Nature 228, 726–739.
22. Rohlfs, R. J., Mathews, A. J., Carver, T. E., Olson, J. S., Springer, B. A., Egeberg, K. D., & Sligar, S. G. (1990) J. Biol. Chem. 265, 3168–3176.
23. Scheidt, W. R., & Chipman, D. M. (1986) J. Am. Chem. Soc. 108, 1163–1167.
24. Smerdon, S. J., Dodson, G. G., Wilkinson, A. J., Gibson, Q. H., Blackmore, R. S., Carver, T. E., & Olson, J. S. (1991) Biochemistry 30, 6252–6260.
25. Springer, B. A., Egeberg, K. D., Sligar, S. G., Rohlfs, R. J., Mathews, A. J., & Olson, J. S. (1989) J. Biol. Chem. 264, 3057–3060.
26. Traylor, T. G., & Stynes, D. V. (1980) J. Am. Chem. Soc. 102, 5939–5941.
27. Traylor, T. G., Chang, C. K., Seibel, I., Berginis, A., Mincey, T., & Cannon, J. (1979) J. Am. Chem. Soc. 101, 6716–6731.
28. Vainshtein, B. K. (1981) in Structural studies on molecules of biological interest (Dodson, G., Glusker, J. P., & Sayre, D., Eds.) Clarendon Press, Oxford, England.