X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
The quinone cofactor TPQ in copper amine oxidase is generated by posttranslational modification of an active site tyrosine residue. Using X-ray crystallography, we have probed the copper-dependent autooxidation process of TPQ in the enzyme from Arthrobacter globiformis. Apo enzyme crystals were anaerobically soaked with copper; the structure determined from this crystal provides a view of the initial state: the unmodified tyrosine coordinated to the bound copper. Exposure of the copper-bound crystals to oxygen led to the formation of freeze-trapped intermediates; structural analyses indicate that these intermediates contain dihydroxyphenylalanine quinone and trihydroxyphenylalanine. These are the first visualized intermediates during TPQ biogenesis in copper amine oxidase.
Kim
Misa
M
School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan.
Okajima
Toshihide
T
Kishishita
Seiichiro
S
Yoshimura
Megumi
M
Kawamori
Asako
A
Tanizawa
Katsuyuki
K
Yamaguchi
Hiroshi
H
D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry* / Q000378:metabolism*; D001051:Apoenzymes / Q000737:chemistry / Q000378:metabolism; D001173:Arthrobacter / Q000201:enzymology; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D013053:Spectrophotometry; D055672:Static Electricity
C086758:2,4,5-trihydroxyphenylalanine quinone; D001051:Apoenzymes; D004295:Dihydroxyphenylalanine; D006631:Amine Oxidase (Copper-Containing)