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Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase

Autor: P N, Turowski, M A, McGuirl, D M, Dooley

Publikováno v: The Journal of biological chemistry. 268(24)

The equilibrium between the two substrate-reduced forms of pea seedling amine oxidase, one containing Cu(II) and reduced 3-(2,4,5-trihydroxyphenyl)-L-alanine (topa) cofactor and one containing Cu(I) and topa semi-quinone, was investigated by visible

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::790a45e524144c86481606b8b3d3c59b
https://pubmed.ncbi.nlm.nih.gov/8349651

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Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases

Autor: D, Mu, S M, Janes, A J, Smith, D E, Brown, D M, Dooley, J P, Klinman

Publikováno v: The Journal of biological chemistry. 267(12)

The recently discovered organic cofactor of bovine serum amine oxidase, topa quinone, is an uncommon amino acid residue in the polypeptide backbone (Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L., and Klinman,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b7a49b157ba7c0d983d1fd1cd29d7d81
https://pubmed.ncbi.nlm.nih.gov/1569055

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The organic functional group in copper-containing amine oxidases. Resonance Raman spectra are consistent with the presence of topa quinone (6-hydroxydopa quinone) in the active site

Autor: D E, Brown, M A, McGuirl, D M, Dooley, S M, Janes, D, Mu, J P, Klinman

Publikováno v: The Journal of biological chemistry. 266(7)

Resonance Raman spectroscopy has been used to probe the structure of the organic cofactor in copper-containing amine oxidases from bovine plasma, porcine kidney, pea seedlings, and the bacterium Arthrobacter P1. The enzymes were first derivatized wit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::84d0dc1cf08ae579e73f2ad4dfb9d588
https://pubmed.ncbi.nlm.nih.gov/1900285

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Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase

Autor: W S, McIntire, D M, Dooley, M A, McGuirl, C E, Cote, J L, Bates

Publikováno v: Journal of neural transmission. Supplementum. 32

Methylamine oxidase (MAOx) from Gram-positive soil bacterium Arthrobacter P1 catalyzes the oxidation of CH3NH2 to H2C = O and NH4+ via reduction of O2 to H2O2. Past work indicates that MAOx is similar to mammalian plasma amine oxidase (PAO) and diami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6fc1bcb0e2562c1f12325ff26352d5b1
https://pubmed.ncbi.nlm.nih.gov/1965196

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Spectroscopic and kinetics studies of the inhibition of pig kidney diamine oxidase by anions

Autor: D M Dooley, K C Golnik

Publikováno v: Journal of Biological Chemistry. 258:4245-4248

The role of copper in pig kidney diamine oxidase has been probed by examining the effects of potential Cu(II) ligands on the spectroscopic and catalytic properties of the enzyme. In the presence of azide and thiocyanate, new absorption bands are evid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::517012229043ff7f0b8b9cfe66cbc478
https://doi.org/10.1016/s0021-9258(18)32613-9

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ChemInform Abstract: MOLECULAR STRUCTURE AND MAGNETIC PROPERTIES OF THE CHLORO-BRIDGED DIMER CHLORO(HYDROTRIS(1-PYRAZOLYL)BORATO)COPPER(II). OBSERVATION OF A FERROMAGNETIC GROUND STATE

Autor: S. G. N. ROUNDHILL, D. M. ROUNDHILL, D. R. BLOOMQUIST, C. LANDEE, R. D. WILLETT, D. M. DOOLEY, H. B. GRAY

Publikováno v: Chemischer Informationsdienst. 10

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ba3cd97ac17a270e419910f0d7b639a0
https://doi.org/10.1002/chin.197925064

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Spectroscopic and kinetics studies of the inhibition of pig kidney diamine oxidase by anions

Autor: D M, Dooley, K C, Golnik

Publikováno v: The Journal of biological chemistry. 258(7)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0c84d00b1b6cb726eb95ac359af266f1
https://pubmed.ncbi.nlm.nih.gov/6403525

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Inactivation of beef plasma amine oxidase by sulfide

Autor: D M, Dooley, C E, Coté

Publikováno v: The Journal of biological chemistry. 259(5)

Sulfide irreversibly inactivates beef plasma amine oxidase in a time-dependent reaction. Mercaptoacetic acid and 2-mercaptoethanol do not inactivate the enzyme. The sulfide complex displayed an intense absorption band at 360 nm (epsilon = 6000 M-1 cm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cf9dd4e9bdab8bf1a65f0f1bf5b5dac7
https://pubmed.ncbi.nlm.nih.gov/6321486

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