Metal coordination influences substrate binding in horseradish peroxidase

European Biophysics Journal

Volumn 29, Issue 6, 2000, Pages 429-438

  Balog, E ^a   Galantai R ^a   Kohler M ^b   Laberge, M ^a   Fidy, J ^a  

^a SEMMELWEIS UNIVERSITY OF MEDICINE   (Hungary)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Horseradish peroxidase; Porphyrin Q band splitting; Protein isothermal compressibility; Spectral hole burning; Stark effect

Indexed keywords

HORSERADISH PEROXIDASE; MAGNESIUM ION; MESOPORPHYRIN;

ARTICLE; COMPARATIVE STUDY; COMPRESSIVE STRENGTH; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; NONHUMAN; PROTEIN STRUCTURE; SPECTROSCOPY;

ARMORACIA RUSTICANA;

EID: 0033803128     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490000084     Document Type: Article

References (36)

1. Interpretation of multiple Q((0,0)) bands in the absorption spectrum of Mg-mesoporphyrin embedded in horseradish peroxidase
2. Thermodynamic fluctuations in protein molecules
3. Horseradish peroxidase structure and kinetic properties
4. The pH dependence of phototautomerization in horseradish peroxidase monitored by fluorescence line narrowing spectroscopy
5. Differences in the binding of aromatic substrates to horseradish peroxidase revealed by fluorescence line narrowing
6. Softening of the packing density of horseradish peroxidase by a H-donor bound near the heme pocket
7. More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. A site selection spectroscopic study
8. Proteins in electric fields and pressure fields: Experimental results
9. Spectral hole burning and selection of conformational substates in chromoproteins
10. Correlation between protein conformation and prosthetic group configuration as tested by pH effects: A hole burning study on mesoporphyrin-IX substituted horseradish peroxidase
11. Structural changes and internal fields in proteins: A hole-burning Stark effect study of horseradish peroxidase
12. Crystal structure of horseradish peroxidase C at 2.15 A resolution
13. Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography
14. Energy landscape of the tautomer states of mesoporhyrin embedded in horseradish peroxidase
15. Peroxidases, catalases and chloroperoxidases
16. Measuring internal electric fields with atomic resolution
17. Stark effect experiments in cytochrome-c type proteins: Structural hierarchies
18. Symmetry breaking by the heme pocket in horseradish peroxidase as revealed by Stark spectroscopy
19. Proteins in electric fields and pressure fields: Basic aspects
20. Intrinsic protein electric fields: Basic non-covalent interactions and relationship to protein-induced Stark effects
21. Probing structural heterogeneities in proteins by high resolution spectroscopy and electrostatic calculations
22. Sampling field heterogeneity at the heme of c-type cytochromes by spectral hole burning spectroscopy and electrostatic calculations
23. Microscopic theory of reversible pressure broadening in hole-burning spectra of impurities in glasses
24. Structural determinants of the catalytic activities of peroxidases
25. Reconstitution of hemeproteins
26. Binding of donors to horseradish peroxidase: A spectroscopic study
27. Protein dynamics at low temperatures
28. New complexes of peroxidases with hydroxamic acids, hydrazides, and amides
29. Understanding heme cavity structure of peroxidases: Comparison of electronic absorption and resonance raman spectra with crystallographic results
30. Cleavage of the haem-protein link by acid methyl ethyl ketone
31. Substrate binding and catalysis in heme peroxidases
32. Aromatic donor molecule binding sites of haem peroxidases
33. 0 So transition of free-base porphyrin in an n-octane crystal as studied by photochemical hole burning
34. Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes
35. Conformational relaxation of a low-temperature protein as probed by photochemical hole burning
36. Photochemical holes under pressure: Compressibility and volume fluctuations of a protein