Biochemical and spectroscopic properties of the four-subunit quinol oxidase (cytochrome ba3) from Paracoccus denitrificans

I. Zickermann, S. Anemuller, O. M. Richter, O. S. Tautu, T. A. Link, B. Ludwig*

*Corresponding author for this work
16 Citations (Scopus)

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 languageEnglish
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1277
Issue number1-2
Pages (from-to)93-102
Number of pages10
ISSN0005-2728
DOIs
Publication statusPublished - 1996

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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