Proximal cysteine residue is essential for the enzymatic activities of cytochrome p450cam

European Journal of Biochemistry

Volumn 268, Issue 2, 2001, Pages 252-259

  Yoshioka, Shiro ^a   Takahashi, Satoshi ^a   Hori, Hiroshi ^b   Ishimori, Koichiro ^a   Morishima, Isao ^a  

^a KYOTO UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

Axial push effect; CPO; Oxygen activation; P420; P450

Indexed keywords

CAMPHOR; CARBON DIOXIDE; CUMENE HYDROPEROXIDE; CYSTEINE; CYTOCHROME P450; HEME; HISTIDINE; IRON; LIGAND; OXYGEN; THIOLATE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; CELL INCLUSION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

EID: 0034836145     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2001.01872.x     Document Type: Article

References (61)

1. Heme-containing oxygenases
2. Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein
3. Chloroperoxi-dase. VII. Classical peroxidatic, catalytic, and halogenating forms of the enzyme
4. Chloroperoxidase: A review
5. Models and mechanisms of cytochrome P450 action
6. cam
7. Stereochemistry of the chloroperoxidase active site: Crystallographic and molecular-modeling studies
8. Magnetic circular dichroism studies. 43. Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism
9. Probing structure-function relations in heme-containing oxygenases and peroxidases
10. cam. II. Interconversion with P420
11. P-450 nature of the carbon monoxide complex of ferrous chloroperoxidase
12. The role of the proximal ligand in heme enzymes
13. Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue
14. Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: Characterization and their catalytic activities
15. Roles of proximal ligand in heme proteins: Replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase
16. Synthesis of a highly stable iron porphyrin coordinated by alkylthiolate anion as a model for cytochrome P450 and its catalytic activity in oxygen-oxygen bond cleavage
17. Heterolytic oxygen-oxygen bond cleavage of peroxy acid and effective alkane hydroxylation in hydrophobic solvent mediated by an iron porphyrin coordinated by thiolate anion as model for cytochrome P-450
18. cam studied with the site-directed mutagenesis at the heme proximal site
19. Structural studies on prokaryotic cytochrome P450
20. Proton-assisted pathway to formation of the catalytically active, ferryl species of P450eryF
21. Theoretical investigation of the proton assisted pathway to formation of cytochrome P450 compound I
22. Roles of the axial ligand in determining the spin state of resting cytochrome P450
23. Evidence for sulfur-based radicals in thiolate compound I intermediates
24. cam gene
25. Site-directed mutagenesis of rat liver cytochrome P-450d: Axial ligand and heme incorporation
26. Rapid and efficient site-specific mutagenesis without phenotypic selection
27. Rapid and efficient site-specific mutagenesis without phenotypic selection
28. cam
29. cam
30. cam methylene monooxygenase components: Cytochrome m, putidare-doxin, and putidaredoxin reductase
31. cam as revealed by site-directed mutagenesis
32. cam monooxygenase system
33. Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: Protein models for the active site of P-450
34. cam mutants
35. cam using one-dimensional and two-dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments
36. cam monooxygenase reaction by a single mutation, threonine-252 to lanine or valine: A possible role of the hydroxy amino acid in oxygen activation
37. The carbon monoxide-binding pigment of liver microsomes
38. Nature of O2 and CO binding to metalloporphyrins and heme proteins
39. Resonance Raman spectroscopy of metalloporphyrins
40. Vibrational modes of coordinated CO, CN2, O2, and NO
41. How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models
42. Studies on the heme environment of oxidized cytochrome b5
43. cam from Pseudomonas putida
44. Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome P450 and P420
45. Nature of the iron-ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering
46. cam mixed function oxidation by putidaredoxin and camphor ligation
47. cam on binding of specific substrates
48. cam
49. cam (CYP101) nitrosyl complexes: Effects of camphor and its analogues on ligand-bound structure
50. Probing the heme iron coordination structure of alkaline chloroperoxidase
51. cam
52. Induced changes in the electron paramagnetic resonance spectra of mammalian catalases
53. cam binding surface as refined by site-directed mutagenesis and electrostatic modeling
54. cam electron transer complex: Identification of the residue responsible for redox-state-dependent conformers
55. cam electron-transfer complex
56. cam Interaction. Spin state of the heme iron modulates putidaredoxin structure
57. ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide