Comparison of inactivation and unfolding of methanol dehydrogenase during denaturation in guanidine hydrochloride and urea

International Journal of Biochemistry and Cell Biology

Volumn 32, Issue 8, 2000, Pages 873-878

  Wang, Guan Fang ^a   Cao, Zhi Fang ^b   Zhou, Hai Meng ^b   Zhao, Yong Fang ^a  

^a WUHAN UNIVERSITY   (China)

^b TSINGHUA UNIVERSITY   (China)

Author keywords

Conformational change; Inactivation; Methanol dehydrogenase

Indexed keywords

GUANIDINE; OXIDOREDUCTASE; QUINONE DERIVATIVE; UREA;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME INACTIVATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; STEADY STATE;

ALCOHOL OXIDOREDUCTASES; BINDING SITES; CALCIUM; DOSE-RESPONSE RELATIONSHIP, DRUG; GUANIDINE; KINETICS; PQQ COFACTOR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; QUINOLONES; QUINONES; SPECTROMETRY, FLUORESCENCE; UREA;

EID: 0034255231     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(00)00027-3     Document Type: Article

References (20)

1. Hauge J.G. Glucose dehydrogenase of bacterium anitratum: an enzyme with a novel prosthetic group. J. Biol. Chem. 239:1964;3630-3639.
2. Anthony C., Zatman L.J. The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group. Biochem. J. 104:1967;960-969.
3. Salisbury S.A., Forrest H.S., Cruse W.B.T., Kennard O.A. novel coenzyme from bacterial primary alcohol dehydrogenases. Nature. 280:1979;843-844.
4. Duine J.A., Frank J., Verwiel P.E.J. Structure and activity of the prosthetic group of methanol dehydrogenase. Eur. J. Biochem. 108:1980;187-192.
5. Anthony C. Bacterial oxidation of methane and methanol. Adv. Microb. Physiol. 27:1986;113-210.
6. Anthony C. Quinoprotein-catalysed reactions. Biochem. J. 320:1996;697-711.
7. Xia Z.X., He Y.N., Dai W.W., White S.A., Cruse W.B.T., Kennard O. Detailed active site configuration of a new crystal form of methanol dehydrogenase from methylophilus W3A1 at 1.9 resolution. Biochemistry. 38:1999;1214-1220.
8. Harms N., Vries G.E., Maurer K., Hoogendijk J., Stouthamer A.H. Protein, Nucleotide Isolation and nucleotide sequence of the methanol dehydrogenase structural gene from Paracoccus denitrificans. J. Bacteriol. 169:1987;3969-3975.
9. Machlin S.M., Hanson R.S. Nucleotide sequence and transcriptional start site of the methylobacterium organophilum XX methanol dehydrogenase structural gene. J. Bacteriol. 170:1988;4739-4747.
10. Tsou C.L. Location of the active sites of some enzymes in limited & flexible molecular regions. Trends Biochem. Sci. 11:1986;427-429.
11. Tsou C.L. Conformational flexibility of enzyme active sites. Science. 262:1993;380-381.
12. Bai J.H., Zheng S.Y., Zhou H.M. Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation. Biochem. Mol. Biol. Int. 45:1998;941-951.
13. He B., Bai J.H., Zhou H.M. Comparison of inactivation and unfolding of yeast alcohol dehydrogenase during thermal denaturation. Int. J. Biochem. Cell Biol. 29:1997;1021-1028.
14. He B., Zhang Y., Zhang T., Wang H.R., Zhou H.M. Inactivation and unfolding of aminoacylase during denaturation in sodium dodecyl sulfate solutions. J. Protein Chem. 14:1995;349-357.
15. Day D.J., Anthony C. Methanol dehydrogenase from methylobacterium extorquens AM1. Methods Enzymol. 188:1990;210-216.
16. Zhao Y.F., Cheng H., Zhang J.W., Wang Y.S. Studies on a new prosthetic group PQQ-dependent methanol dehydrogenase. J. Wuhan Univ. 45:1999;243-246.
17. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
18. Kamoun P.P. Denaturation of globular proteins by urea: breakdown of hydrogen or hydrophobic bonds? Trends Biochem. Sci. 13:1988;424-425.
19. Hagihara Y., Tan Y., Goto Y. Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride. J. Mol. Biol. 237:1994;336-348.
20. Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzyol. 131:1986;266-280.