proton transfer occurs predominantly to oxygen O2 of D128 in beta subunit in a reaction dominated by tunneling over 0.6 Angstroms. Tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required
two mol of heme per mole of AMDH, 60 kDa subunit carries heme c. Typical absorption stectrum shows maxima at 554, 522, 420, and 320 nm in the reduced state and one peak at 410 nm, a shoulder at 350 nm, and a braod hill at 530 nm in the oxidized form
Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. [Erratum to document cited in CA144:14530]
Hothi, P.; Lee, M.; Cullis, P.M.; Leys, D.; Scrutton, N.S.
Catalysis by the isolated tryptophan tryptophylquinone-containing subunit of aromatic amine dehydrogenase is distinct from native enzyme and synthetic model compounds and allows further probing of TTQ mechanism