Biochemical and spectroscopic properties of the four-subunit quinol oxidase (cytochrome ba3) from Paracoccus denitrificans.
The ba3 quinol oxidase from Paracoccus denitrificans has been purified by a new protocol leading to significantly higher yields than previously reported (Richter et al. (1994) J. Biol. Chem. 269, 23079-23086). In an SDS PAG an additional protein band compared with the previous preparation appears, which can be identified as the major form of subunit II. All protein bands can be assigned to genes of the qox operon by N-terminal sequencing, indicating that the oxidase consists of four subunits. In addition to one heme A, one heme B, and one copper atom, the preparation contains two ubiquinone molecules per enzyme. The oxidase is further characterized by electron paramagnetic resonance (EPR), circular dichroism (CD) and magnetic circular dichroism (MCD) spectroscopy.
Zickermann
I
I
Institute of Biochemistry/Molecular Genetics, University of Frankfurt, Germany.
Anemüller
S
S
Richter
O M
OM
Tautu
O S
OS
Link
T A
TA
Ludwig
B
B
D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D008280:Magnetics; D016297:Mutagenesis, Site-Directed; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010231:Paracoccus denitrificans / Q000201:enzymology*; D011499:Protein Processing, Post-Translational
D010088:Oxidoreductases; C020094:duroquinol oxidase