Activity and conformational changes of horseradish peroxidase in trifluoroethanol

Biochemistry and Cell Biology

Volumn 80, Issue 2, 2002, Pages 205-213

  Zhou, Hong Wei ^a   Xu, Yan ^a   Zhou, Hai Meng ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

Horseradish peroxidase; Soret; Trifluoroethanol; Unfolding

Indexed keywords

ABSORPTION; BIOASSAY; CONFORMATIONS; ELECTROPHORESIS; ENZYMES; ETHANOL; HYDROPHOBICITY; MOLECULAR BIOLOGY;

CIRCULAR DICHROISM (CD);

BIOCHEMISTRY;

HORSERADISH PEROXIDASE; TRIFLUOROETHANOL; UREA;

ALPHA HELIX; ARTICLE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; DENATURATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME INACTIVATION; INCUBATION TIME; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SPECTRAL SENSITIVITY; SURFACE CHARGE;

BINDING SITES; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GUANIDINE; HORSERADISH PEROXIDASE; HYDROGEN BONDING; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SPECTROMETRY, FLUORESCENCE; TRIFLUOROETHANOL; TRYPSINOGEN; UREA;

ARMORACIA RUSTICANA;

EID: 0036203881     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o02-003     Document Type: Article

References (39)

1. Haem propionates control oxidative and reductive activities of horseradish peroxisase by maintaining the correct orientation of the haem
2. Hydrophobic solvation in aqueous trifluoroethanol solution
3. Intramolecular tryptophan heme energy transfer in horseradish peroxidase
4. Rates of reaction of indoleacetic acids with horseradish peroxidase compound I and their dependence on the redox potentials
5. pH dependence of the active site of horseradish peroxidase compound II
6. Structure and conformational stability of horseradish peroxidase: Effect of temperature and pH
7. The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen
8. pH-induced confromational perturbaion in horseradish peroxidase
9. Probing structure-function relations in heme-containing oxygenases and peroxidases
10. Crystal structure of horseradish peroxidase C at 2.15 Å resolution
11. Amperometric sensors for peroxide, choline, and acetylcholine based on electron transfer between horseradish peroxidase and a redox polymer
12. Trifluoroethanol-induced conformational transitions of proteins: Insights gained from the differences between α-lactalbumin and ribonuclease A
13. Tryptophanless recombinant horseradish peroxidase stability and catalytic properties
14. The reaction rate of NO with horseradish peroxidase compound I and II
15. Structural interacitons between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography
16. Chimeric molecules employing horseradish peroxidase as reporter enzyme for protein localization in the electron microscope
17. Mutation of distal residues of horseradish peroxidase: Influence on substate binding and cavity properties
18. Reactivation and refolding of rabbit muscle creatine kinase denatured in 2,2,2,-trifluoroethanol solutions
19. Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome c
20. Apohorseradish peroxidase unfolding and refolding: Intrinsic tryptophan fluorescence studies
21. Trifluoroethanol stabilizes the pH 4 folding intermediated of sperm whale apomyoglobin
22. Does trifluoroethanol affect folding pathways and can it be used as a probe of structure in transition states?
23. Denaturation of horseradish peroxidase with urea and guanidine hydrochloride
24. A step towards understanding the folding mechanism of horseradish peroxidase tryptophan fluorescence and circular dichroism equilibrium studies
25. A model for the interaction of trifluoroethanol with peptides and proteins
26. Role of arginine 38 in horseradish peroxidase
27. Reactivity of horseradish peroxidase compound II toward substrates: Kinetic evidence for a two-step mechanism
28. How do organic solvents affect peroxidase structure and function
29. Improvement of peroxidase activity by relocation of a catalytic histidine within the active site of horseradish peroxidase
30. Presence of endogenous calcium ion and its functional and structual regualtion in horseradish peroxidase
31. Spectroscopic evidence for a conformational transition in horseradish peroxidase at very low pH
32. Hydrogen bond network in the distal site of peroxidase: Spectroscopic properties of Asn70-Asp horseradish peroxidase mutant
33. Catalytic activities and structural properties of horseradish peroxidase distal His42-Glu or Gln mutant
34. Conformational states in denaturants of cytochrome c and horse-radish peroxidase examined by fluorescence and circular dichroism
35. Two-dimentional 1H-NMR studies of horseradish peroxidase C and interaction with indole-3-propionic acid
36. Conformational changes of active sites during refolding of urea-denatured creatine kinase
37. Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride