A continuous-wave electron-nuclear double resonance (X-band) study of the Cu2+ sites of particulate methane mono-oxygenase of methylococcus capsulatus (strain M) in membrane and pure dopamine β-mono-oxygenase of the adrenal medulla

Biochemical Journal

Volumn 363, Issue 3, 2002, Pages 677-686

  Katterle, Bettina ^a   Gvozdev, Rudolf I ^a   Abudu, Ntei ^a   Ljones, Torbjørn ^a   Andersson, K Kristoffer ^a  

^a UNIVERSITY OF OSLO   (Norway)

Author keywords

CW ENDOR; Dopamine mono oxygenase; Methane mono oxygenases; Type 2 copper site

Indexed keywords

BACTERIA; CHELATION; COMPUTER SIMULATION; ENZYMES; PARAMAGNETIC RESONANCE; PROTONS;

MEMBRANE FRAGMENTS;

BIOCHEMISTRY;

AMMONIA; AZIDE; CHELATING AGENT; COPPER ION; CYANIDE; DEUTERIUM OXIDE; DIETHYLDITHIOCARBAMIC ACID; DOPAMINE BETA MONOOXYGENASE; ENZYME INHIBITOR; FERRICYANIDE; HISTIDINE; METHANE MONOOXYGENASE; NITROGEN;

ADRENAL MEDULLA; ARTICLE; BACTERIAL MEMBRANE; CHELATION; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME PURIFICATION; METHYLOCOCCUS CAPSULATUS; MICROWAVE RADIATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL;

ADRENAL MEDULLA; ANIMALS; COPPER; DOPAMINE BETA-HYDROXYLASE; ELECTRON SPIN RESONANCE SPECTROSCOPY; METHYLOCOCCUS CAPSULATUS; OXIDATION-REDUCTION; OXYGENASES;

BACTERIA (MICROORGANISMS); METHYLOCOCCUS; METHYLOCOCCUS CAPSULATUS;

EID: 0036566432     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3630677     Document Type: Article

References (41)

1. Mechanisms whereby mononuclear copper proteins functionalize organic substrates
2. Dioxygen activation by enzymes containing binuclear non-heme iron clusters
3. The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath)
4. The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methytococcus capsulatus (Bath)
5. Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
6. The role of copper in particulate methane monooxygenase from Methylosinus trichosporium OB3b
7. 2+ in pMMO from Methylomicrobium album BG8
8. Low-frequency EPR of the copper in particulate methane monooxygenase from Methylomicrobium albus BG8
9. Pulsed EPR studies of particulate methane monooxygenase from Methylococcus capsulatus (Bath): Evidence for histidine ligation
10. The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme: Isolation and characterization
11. X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxygenase from Methylococcus capsulatus (Bath). Cu(I) ions and their implications
12. Kinetic studies on the activation of dopamine β-monooxygenase by copper and vanadium ions
13. Sequence similarity between dopamine β-hydroxylase and peptide α-amidating enzyme: Evidence for a conserved catalytic domain
14. Amidation of bioactive peptides: The structure of peptidylglycine α-hydroxylating monooxygenase
15. The catalytic core of peptidylglycine α-hydroxylating monooxygenase: Investigation by site-directed mutagenesis, Cu X-ray-absorption spectroscopy, and electron-paramagnetic-resonance
16. Peptidylglycine α-hydroxylating monooxygenase: Active site residues, disulfide linkages, and a two-domain model of the catalytic core
17. Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine α-amidating enzyme
18. Active-site of dopamine β-hydroxylase: Comparison of enzyme derivatives containing 4 and 8 copper atoms per tetramer using potentiometry and electron-paramagnetic-resonance-spectroscopy
19. Kinetic and electron-paramagnetic-resonance studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) β-monooxygenase
20. ELectron spin-echo studies of the copper(II) binding-sites in dopamine β-hydroxylase
21. Copper K-extended X-ray absorption fine-structure studies of oxidized and reduced dopamine β-hydroxylase: Confirmation of a sulfur ligand to copper(I) in the reduced enzyme
22. Investigation of the copper centre of membrane-bound methane monooxygenase from subcellular structures of Methylococcus capsulatus (Strain M)
23. Solubilization of methane monooxygenase from Methylococcus capsulatus (Bath)
24. Electron nuclear double resonance
25. Electron paramagnetic resonance with applications to selected problems in biology
26. ESR and ENDOR of Cu(II) complexes with nitrogen donors: Probing parameters for prosthetic group modeling of superoxide dismutase
27. ENDOR of superoxide dismutase: Structure determination of the copper site from randomly oriented specimen
28. Concentration of Cu, EPR-detectable Cu, and formation of cupric-ferrocyanide in membranes with pMMO
29. Dopamine β-hydroxylase: Electron-paramagnetic resonance and oxidation-reduction properties of enzyme-bound copper
30. Multicopper oxidases and oxygenases
31. ENDOR and ESEEM studies of cytochrome-c-oxidase: Evidence for exchangeable protons at the Cu(A) site
32. Structure at 2.8 Angstrom resolution of cytochrome-c-oxidase from Paracoccus denitrificans
33. Structures of metal sites of oxidized bovine heart cytochrome-c-oxidase at 2.8 Angstrom
34. An ENDOR study of human and bovine erythrocyte superoxide dismutase: H-1 and N-14 interactions
35. 2O
36. The structure of the active center of β-peptide in membrane-bound methane monooxygenase (pMMO) from Methylococcus capsulatus Bath
37. High-frequency electron paramagnetic resonance spectroscopy of the apogalactose oxidase radical
38. A metalloradical mechanism for the generation of oxygen from water in photosynthesis
39. Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244
40. Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide