Heme crevice disorder after sixth ligand displacement in the cytochrome c-551 family

Archives of Biochemistry and Biophysics

Volumn 457, Issue 1, 2007, Pages 95-104

  Chen, Yinghua ^a   Liang, Qiaoli ^a   Arciero, David M ^b   Hooper, Alan B ^b   Timkovich, Russell ^a  

^a UNIVERSITY OF ALABAMA   (United States)

^b UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Alkaline transition; Cyanide complex; Cytochrome c 551; Heme crevice; Heterogeneity; Methionine ligand

Indexed keywords

CYTOCHROME C; HEME; HEMOPROTEIN; LIGAND; METHIONINE; MITOCHONDRIAL PROTEIN; POTASSIUM CYANIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE);

ABSORPTION SPECTROSCOPY; ALKALINITY; ARTICLE; BACTERIAL STRAIN; CHEMICAL REACTION; CONTROLLED STUDY; HEATING; ISOMER; KINETICS; LOW TEMPERATURE; MITOCHONDRION; NITROSOMONAS EUROPAEA; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEFECT; PROTON NUCLEAR MAGNETIC RESONANCE; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS STUTZERI; THERMODYNAMICS; TIME;

BACTERIAL PROTEINS; CYTOCHROME C GROUP; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; HYDROGEN-ION CONCENTRATION; LIGANDS; METHIONINE; NITROSOMONAS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; POTASSIUM CYANIDE; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PSEUDOMONAS;

NITROSOMONAS; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS STUTZERI;

EID: 33845711162     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2006.10.001     Document Type: Article

References (43)

1. Moore G.R., and Pettigrew G.W. Cytochromes c: Evolutionary, Structural, and Physiochemical Aspects (1990), Springer-Verlag, Berlin
2. Cai M., Bradford E.G., and Timkovich R. Biochemistry 31 (1992) 8603-8612
3. Dohler K., Huss V.A.R., and Zumft W.G. Int. J. Syst. Bacteriol. 37 (1987) 1-3
4. Arciero D.M., Peng Q., Peterson J., and Hooper A.B. FEBS Lett. 342 (1994) 217-220
5. Miller G.T., Zhang B., Hardman J.K., and Timkovich R. Biochemistry 39 (2000) 9010-9017
6. Miller G.T., Mackay D.Q., Standley M.S., Fields S.I., Clary W.M., and Timkovich R. Protein Express. Purif. 29 (2003) 244-251
7. Zhong L., Wen X., Rabinowitz T.M., Russell B.S., Karan E.F., and Bren K.L. Proc. Nat. Acad. Sci. 101 (2004) 8637-8642
8. Timkovich R., Cai M., Arciero D.M., and Hooper A.B. Eur. J. Biochem. 226 (1994) 159-168
9. Timkovich R., Cork M.S., and Taylor P.V. Biochemistry 23 (1984) 3526-3533
10. Keller R.M., Pettigrew G.W., and Wuthrich K. FEBS Lett. 36 (1973) 151-156
11. Hon-Nami K., Kihara H., Kitagawa T., Miyazawa T., and Oshima T. Eur. J. Biochem. 110 (1980) 217-223
12. Tachiiri N., Hemmi H., Takayama S.J., Mita H., Hasegawa J., Sambongi Y., and Yamamoto Y. J. Biol. Inorg. Chem. 9 (2004) 733-742
13. Blanchard L., Marion D., Pollock B., Voordouw G., Wall J., Bruschi M., and Guerlesquin F. Eur. J. Biochem. 218 (1993) 292-301
14. Wen X., and Bren K.L. Biochemistry 44 (2005) 5225-5233
15. Wen X., and Bren K.L. Inorg. Chem. 44 (2005) 8587-8593
16. Keller R.M., Schejter A., and Wuthrich K. Biochim. Biophys. Acta 626 (1980) 15-22
17. Yamamoto Y., Nanai N., Inoue Y., and Chujo R. Biochem. Biophys. Res. Comm. 151 (1988) 262-269
18. Chau M.H., Cai M., and Timkovich R. Biochemistry 29 (1990) 5076-5087
19. Timkovich R., Bergmann D., Arciero D.M., and Hooper A.B. Biophys. J. 75 (1998) 1964-1972
20. Karan E.F., Russell B.S., and Bren K.L. J. Biol. Inorg. Chem. 7 (2002) 260-272
21. George P., and Tsou C.L. Biochem. J. 50 (1952) 440-448
22. Dyer C., Schubert A., Feinberg B.A., and Timkovich R. Biochim. Biophys. Acta 579 (1979) 253-268
23. Matsuura Y., Takano T., and Dickerson R.E. J. Mol. Biol. 156 (1982) 389-409
24. Cai M., and Timkovich R. Biochem. Biophys. Res. Comm. 254 (1999) 675-678
25. Banci L., Bertini I., Bren K.L., Gray H.B., Sompornpisut P., and Turano P. Biochemistry 34 (1995) 11385-11398
26. Yao Y., Qian C., Ye K., Wang J., Bai Z., and Tang W. J. Biol. Inorg. Chem. 7 (2002) 539-547
27. Chao Y.Y.H., Bersohn R., and Aisen P. Biochemistry 18 (1979) 774-779
28. Li Y., Imaeda K., and Inokuchi H. J. Phys. Chem. 98 (1994) 4726-4728
29. Cutruzzola F., Ciabatti I., Roll G., Falcinelli S., Arese M., Ranghino G., Anselmino A., Zennaro E., and Silvestrini M.C. Biochem. J. 322 (1997) 35-42
30. Timkovich R., and Cai M. Biochemistry 32 (1993) 11516-11523
31. Timkovich R., Cai M., and Dixon D.W. Biochem. Biophys. Res. Commun. 150 (1988) 1044-1050
32. Jimenez H.R., Pardal C., and Moratal J.M. Polyhedron 24 (2005) 1813-1820
33. Cai M., and Timkovich R. FEBS Lett. 311 (1992) 213-216
34. Stellwagen E., and Cass R.D. J. Biol. Chem. 250 (1975) 2095-2098
35. Cho K.C., Chu W.F., Choy C.L., and Che C.M. Biochim. Biophys. Acta 934 (1988) 161-168
36. Ragg E., and Moore G.R. J. Inorg. Biochem. 21 (1984) 253-261
37. Eley C.G.S., Moore G.R., Williams G., and Williams R.J.P. Eur. J. Biochem. 124 (1982) 295-303
38. McCray J.A., and Kihara T. Biochim. Biophys. Acta 548 (1979) 417-426
39. Ilan Y., and Shafferman A. Biochim. Biophys. Acta 548 (1979) 161-165
40. Andersson T., Thulin E., and Forsen S. Biochemistry 18 (1979) 2487-2493
41. Hasegawa J., Yoshida T., Yamazaki T., Sambongi S., Yu Y., Igarashi Y., Kodama T., Yamazaki H., Kyogoku Y., and Kobayashi Y. Biochemistry 37 (1998) 9641-9649
42. Bren K.L., Kellogg J.A., Kaur R., and Wen X. Inorg. Chem. 43 (2004) 7934-7944
43. Takahasha Y., Takayama S.J., Mikami S., Mita H., Sambongi Y., and Yamamoto Y. Chem. Lett. 35 (2006) 528-529