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

doi:10.1016/S0005-2728(96)00086-2

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^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biochemie

Johann Wolfgang Goethe-Universität

16 Zitate (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.

Originalsprache	Englisch
Zeitschrift	Biochimica et Biophysica Acta - Bioenergetics
Jahrgang	1277
Ausgabenummer	1-2
Seiten (von - bis)	93-102
Seitenumfang	10
ISSN	0005-2728
DOIs	https://doi.org/10.1016/S0005-2728(96)00086-2
Publikationsstatus	Veröffentlicht - 1996

Fördermittel

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.

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Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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10.1016/S0005-2728(96)00086-2

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@article{bec0aa08344b43f1bb2ecce67e17756e,

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

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.",

author = "I. Zickermann and S. Anemuller and Richter, \{O. M.\} and Tautu, \{O. S.\} and Link, \{T. A.\} and B. Ludwig",

note = "Funding Information: We thank Herrmann Sch\textasciitilde{}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. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.",

year = "1996",

doi = "10.1016/S0005-2728(96)00086-2",

language = "English",

volume = "1277",

pages = "93--102",

journal = "Biochimica et Biophysica Acta - Bioenergetics",

issn = "0005-2728",

publisher = "Elsevier B.V.",

number = "1-2",

}

Biochemical and spectroscopic properties of the four-subunit quinol oxidase (cytochrome ba₃) from Paracoccus denitrificans. / Zickermann, I.; Anemuller, S.; Richter, O. M. et al.
in: Biochimica et Biophysica Acta - Bioenergetics, Jahrgang 1277, Nr. 1-2, 1996, S. 93-102.

Publikation: Beiträge in Fachzeitschriften › Zeitschriftenaufsätze › Forschung › Begutachtung

TY - JOUR

T1 - Biochemical and spectroscopic properties of the four-subunit quinol oxidase (cytochrome ba3) from Paracoccus denitrificans

AU - Zickermann, I.

AU - Anemuller, S.

AU - Richter, O. M.

AU - Tautu, O. S.

AU - Link, T. A.

AU - Ludwig, B.

N1 - Funding Information: 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. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.

PY - 1996

Y1 - 1996

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0029967914

U2 - 10.1016/S0005-2728(96)00086-2

DO - 10.1016/S0005-2728(96)00086-2

M3 - Journal articles

C2 - 8950374

AN - SCOPUS:0029967914

SN - 0005-2728

VL - 1277

SP - 93

EP - 102

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

IS - 1-2

ER -