Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 268, Issue 2, Pages 470-476Publisher
BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1432-1033.2001.01912.x
Keywords
bioelectrocatalysis; cytochrome c-550; Paracoccus denitrificans; quinohemoprotein amine dehydrogenase; respiratory chain
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The physiological electron acceptor of quinohemoprotein amine dehydrogenase (QH-AmDH) from Paracoccus denitrificans IFO 12442 was identified by biochemical and electrochemical methods. Of three types of heme c-containing proteins purified together with QH-AmDH from the periplasm of n-butylamine-grown cells, only constitutive cytochrome c-550 was reduced by the addition of QH-AmDH and n-butylamine. Reconstitution of the respiratory chain revealed that cytochrome c-550 mediates the electron transfer from QH-AmDH to the terminal oxidase. This is a new pathway of the amine oxidation respiratory chain of P. denitrificans.
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