Abstract
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 FAG 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.
| Original language | English |
|---|---|
| Journal | Biochimica et Biophysica Acta - Bioenergetics |
| Volume | 1277 |
| Issue number | 1-2 |
| Pages (from-to) | 93-102 |
| Number of pages | 10 |
| ISSN | 0005-2728 |
| DOIs | |
| Publication status | Published - 1996 |
Funding
We thank Herrmann Sch~igger for N-terminal sequencing, Axel Wittershagen for metal determinations by total reflection X-ray fluorescence, Miguel Teixeras for cooperation in EPR spectroscopy, and Oliver Hatzfeld for help with optical spectroscopy. Dodecyl ethoxysulfate was kindly provided by Henkel AG (Diisseldorf). The technical assistance of Inge Pecher is gratefully acknowledged as well as the atomic absorption measurements performed by Doris Bergmann-DiSrr. We thank Volker Zickermann for critical discussions. This work was supported by Deutsche Forschungsgemeinschaft (SFB 169 and Li 474/2 to T.A.L.), Graduiertenkolleg 'Pro-teinstrukturen, Dynamik und Funktion', and Fonds der Chemischen Industrie.
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
