Metal-activated histidine carbon donor hydrogen bonds contribute to metalloprotein folding and function

Journal of Inorganic Biochemistry

Volumn 103, Issue 7, 2009, Pages 1054-1060

  Schmiedekamp, Ann ^a   Nanda, Vikas ^b,c  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^c RUTGERS UNIVERSITY   (United States)

Author keywords

DFT; Histidine; Hydrogen bond; Metalloprotein; Superoxide reductase

Indexed keywords

HISTIDINE; IMIDAZOLE; METALLOPROTEIN; WATER;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; HYDROGEN BOND; MOLECULAR INTERACTION; OXIDATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE;

CARBON; CATALYTIC DOMAIN; HISTIDINE; HYDROGEN BONDING; IMIDAZOLES; METALLOPROTEINS; METALS; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN FOLDING; PYROCOCCUS FURIOSUS;

EID: 67449113526     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2009.04.017     Document Type: Article

References (42)

1. Wells J.A., Cunningham B.C., Graygar T.P., and Estell D.A. Philos. Trans. Roy Soc. Lond. A 317 (1986) 415-423
2. Robertus J.D., Kraut J., Alden R.A., and Birktoft J.J. Biochemistry 11 (1972) 4293-4303
3. Jencks W.P. Catalysis in Chemistry, Enzymology (1969), McGraw-Hill, New York
4. Wahl M.C., and Sundaralingam M. Trends Biochem. Sci. 22 (1997) 97-102
5. Ho B.K., and Curmi P.M. J. Mol. Biol. 317 (2002) 291-308
6. Aravinda S., Shamala N., Bandyopadhyay A., and Balaram P. J. Am. Chem. Soc. 125 (2003) 15065-15075
7. Senes A., Ubarretxena-Belandia I., and Engelman D.M. Proc. Natl. Acad. Sci. USA 98 (2001) 9056-9061
8. Ash E.L., Sudmeier J.L., Day R.M., Vincent M., Torchilin E.V., Haddad K.C., Bradshaw E.M., Sanford D.G., and Bachovchin W.W. Proc. Natl. Acad. Sci. USA 97 (2000) 10371-10376
9. Derewenda Z.S., Derewenda U., and Kobos P.M. J. Mol. Biol. 241 (1994) 83-93
10. Scheiner S., Kar T., and Gu Y.L. J. Biol. Chem. 276 (2001) 9832-9837
11. Scheiner S., Kar T., and Pattanayak J. J. Am. Chem. Soc. 124 (2002) 13257-13264
12. Nanda V., and Schmiedekamp A. Proteins Struct. Funct. Bioinf. 70 (2008) 489-497
13. Buncel E., and Onyido I. J. Labelled Compd. Rad. 45 (2002) 291-306
14. Buncel E., Clement O., and Onyido I. Acc. Chem. Res. 33 (2000) 672-678
15. Harding M.M. Acta Crystallogr. D Biol. Crystallogr. 55 Pt 8 (1999) 1432-1443
16. Berman H.M., Westbrook J., Feng Z., Gilliland G., Bhat T.N., Weissig H., Shindyalov I.N., and Bourne P.E. Nucleic Acids Res. 28 (2000) 235-242
17. Adams M.W., Jenney Jr. F.E., Clay M.D., and Johnson M.K. J. Biol. Inorg. Chem. 7 (2002) 647-652
18. Katona G., Carpentier P., Niviere V., Amara P., Adam V., Ohana J., Tsanov N., and Bourgeois D. Science 316 (2007) 449-453
19. Yeh A.P., Hu Y., Jenney Jr. F.E., Adams M.W., and Rees D.C. Biochemistry 39 (2000) 2499-2508
20. Silaghi-Dumitrescu R., Silaghi-Dumitrescu I., Coulter E.D., and Kurtz Jr. D.M. Inorg. Chem. 42 (2003) 446-456
21. Clay M.D., Jenney Jr. F.E., Hagedoorn P.L., George G.N., Adams M.W., and Johnson M.K. J. Am. Chem. Soc. 124 (2002) 788-805
22. Wang G., and Dunbrack Jr. R.L. Nucleic Acids Res. 33 (2005) W94-W98
23. Wang G., and Dunbrack Jr. R.L. Bioinformatics 19 (2003) 1589-1591
24. Jaguar ver. 5.5 and 6.5, Schroedinger, LLC, Portland, Oregon, 2003 and 2006.
25. Hay P.J., and Wadt W.R. J. Chem. Phys. 82 (1985) 299-310
26. Ditchfield R., Hehre W.J., and Pople J.A. J. Chem. Phys. 54 (1971) 724
27. Pudzianowski A.T. J. Phys. Chem. 100 (1996) 4781-4789
28. Gu Y., Kar T., and Scheiner S. J. Mol. Struct. 552 (2000) 17-31
29. Scheiner S. J. Phys. Chem. B 109 (2005) 16132-16141
30. Boys S.B., and Bernardi F. Mol. Phys. 19 (1970) 553-566
31. Sweigart D.A., and O'Brien P. Inorg. Chem. 24 (1985) 1405-1409
32. Brewer C., Brewer G., Luckett C., Marbury G.S., Viragh C., Beatty A.M., and Scheidt W.R. Inorg. Chem. 43 (2004) 2402-2415
33. Yerushalmi R., Brandis A., Rosenbach-Belkin V., Baldridge K.K., and Scherz A. J. Phys. Chem. A 110 (2006) 412-421
34. Taylor R., and Kennard O. J. Am. Chem. Soc. 104 (1982) 5063-5070
35. Dudev T., Lin Y.L., Dudev M., and Lim C. J. Am. Chem. Soc. 125 (2003) 3168-3180
36. Yamashita M.M., Wesson L., Eisenman G., and Eisenberg D. Proc. Natl. Acad. Sci. USA 87 (1990) 5648-5652
37. Word J.M., Lovell S.C., Richardson J.S., and Richardson D.C. J. Mol. Biol. 285 (1999) 1735-1747
38. Garrett T.P., Clingeleffer D.J., Guss J.M., Rogers S.J., and Freeman H.C. J. Biol. Chem. 259 (1984) 2822-2825
39. Maglio O., Nastri F., Pavone V., Lombardi A., and DeGrado W.F. Proc. Natl. Acad. Sci. USA 100 (2003) 3772-3777
40. Babor M., Greenblatt H.M., Edelman M., and Sobolev V. Proteins Struct. Funct. Bioinf. 59 (2005) 221-230
41. Calhoun J.R., Nastri F., Maglio O., Pavone V., Lombardi A., and DeGrado W.F. Biopolymers 80 (2005) 264-278
42. Wade H., Stayrook S.E., and DeGrado W.F. Angew. Chem. Int. Edit. 45 (2006) 4951-4954