A cytochrome aa3-type quinol oxidase from Desulfurolobus ambivalens, the most acidophilic archaeon

S. Anemüller; C. L. Schmidt; I. Pacheco; G. Schäfer; M. Teixeira

doi:10.1111/j.1574-6968.1994.tb06779.x

A cytochrome aa₃-type quinol oxidase from Desulfurolobus ambivalens, the most acidophilic archaeon

S. Anemüller^*, C. L. Schmidt, I. Pacheco, G. Schäfer, M. Teixeira

^*Corresponding author for this work

Institute of Biochemistry

Instituto de Tecnologia Quimica e Biologica - Univesidade Nova de Lisboa

Abstract

Membranes of the extremely thermoacidophilic archaeon Desulfurolobus ambivalens grown under aerobic conditions contain a quinol oxidase of the cytochrome aa₃-type as the most prominent hemoprotein. The partially purified enzyme consists of three polypeptide subunits with apparent molecular masses of 40, 27 and 20 kDa and contains two heme A molecules and one copper atom. CO difference spectra suggest one heme to be a heme a₃-centre. The EPR spectra indicate the presence of a low-spin and a high-spin heme species. Redox titrations of the solubilized enzyme show the presence of two reduction processes, with apparent potentials of + 235 and + 330 mV. The enzyme cannot oxidize reduced cytochrome c, but rather serves as an oxidase of caldariella quinone. Due to their very simple composition, D. ambivalens cell appear as a promising candidate to study Structure-function relationships of cytochrome aa₃ in the integral membrane state.

Original language	English
Journal	FEMS Microbiology Letters
Volume	117
Issue number	3
Pages (from-to)	275-280
Number of pages	6
ISSN	0378-1097
DOIs	https://doi.org/10.1111/j.1574-6968.1994.tb06779.x
Publication status	Published - 15.04.1994

Funding

This work was supported by EEC project BIO2-CT 93-0274, grants from the Deutsche Forschungsgemeinschaft (to S.A. and G.S.) and JNICT, Portugal (grant STRDA/C/BIO/416/ 92). The authors would like to thank Prof. A.V. Xavier for critical discussion of the manuscript.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Areas and Centers

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

Access to Document

10.1111/j.1574-6968.1994.tb06779.x

Cite this

@article{ecc1059d36b7459b94f4dbd4ae8c0bf0,

title = "A cytochrome aa3-type quinol oxidase from Desulfurolobus ambivalens, the most acidophilic archaeon",

abstract = "Membranes of the extremely thermoacidophilic archaeon Desulfurolobus ambivalens grown under aerobic conditions contain a quinol oxidase of the cytochrome aa3-type as the most prominent hemoprotein. The partially purified enzyme consists of three polypeptide subunits with apparent molecular masses of 40, 27 and 20 kDa and contains two heme A molecules and one copper atom. CO difference spectra suggest one heme to be a heme a3-centre. The EPR spectra indicate the presence of a low-spin and a high-spin heme species. Redox titrations of the solubilized enzyme show the presence of two reduction processes, with apparent potentials of + 235 and + 330 mV. The enzyme cannot oxidize reduced cytochrome c, but rather serves as an oxidase of caldariella quinone. Due to their very simple composition, D. ambivalens cell appear as a promising candidate to study Structure-function relationships of cytochrome aa3 in the integral membrane state.",

author = "S. Anem{\"u}ller and Schmidt, \{C. L.\} and I. Pacheco and G. Sch{\"a}fer and M. Teixeira",

note = "Funding Information: This work was supported by EEC project BIO2-CT 93-0274, grants from the Deutsche Forschungsgemeinschaft (to S.A. and G.S.) and JNICT, Portugal (grant STRDA/C/BIO/416/ 92). The authors would like to thank Prof. A.V. Xavier for critical discussion of the manuscript. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.",

year = "1994",

month = apr,

day = "15",

doi = "10.1111/j.1574-6968.1994.tb06779.x",

language = "English",

volume = "117",

pages = "275--280",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

publisher = "Oxford University Press",

number = "3",

}

TY - JOUR

T1 - A cytochrome aa3-type quinol oxidase from Desulfurolobus ambivalens, the most acidophilic archaeon

AU - Anemüller, S.

AU - Schmidt, C. L.

AU - Pacheco, I.

AU - Schäfer, G.

AU - Teixeira, M.

N1 - Funding Information: This work was supported by EEC project BIO2-CT 93-0274, grants from the Deutsche Forschungsgemeinschaft (to S.A. and G.S.) and JNICT, Portugal (grant STRDA/C/BIO/416/ 92). The authors would like to thank Prof. A.V. Xavier for critical discussion of the manuscript. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

PY - 1994/4/15

Y1 - 1994/4/15

N2 - Membranes of the extremely thermoacidophilic archaeon Desulfurolobus ambivalens grown under aerobic conditions contain a quinol oxidase of the cytochrome aa3-type as the most prominent hemoprotein. The partially purified enzyme consists of three polypeptide subunits with apparent molecular masses of 40, 27 and 20 kDa and contains two heme A molecules and one copper atom. CO difference spectra suggest one heme to be a heme a3-centre. The EPR spectra indicate the presence of a low-spin and a high-spin heme species. Redox titrations of the solubilized enzyme show the presence of two reduction processes, with apparent potentials of + 235 and + 330 mV. The enzyme cannot oxidize reduced cytochrome c, but rather serves as an oxidase of caldariella quinone. Due to their very simple composition, D. ambivalens cell appear as a promising candidate to study Structure-function relationships of cytochrome aa3 in the integral membrane state.

AB - Membranes of the extremely thermoacidophilic archaeon Desulfurolobus ambivalens grown under aerobic conditions contain a quinol oxidase of the cytochrome aa3-type as the most prominent hemoprotein. The partially purified enzyme consists of three polypeptide subunits with apparent molecular masses of 40, 27 and 20 kDa and contains two heme A molecules and one copper atom. CO difference spectra suggest one heme to be a heme a3-centre. The EPR spectra indicate the presence of a low-spin and a high-spin heme species. Redox titrations of the solubilized enzyme show the presence of two reduction processes, with apparent potentials of + 235 and + 330 mV. The enzyme cannot oxidize reduced cytochrome c, but rather serves as an oxidase of caldariella quinone. Due to their very simple composition, D. ambivalens cell appear as a promising candidate to study Structure-function relationships of cytochrome aa3 in the integral membrane state.

UR - https://www.scopus.com/pages/publications/85085672944

U2 - 10.1111/j.1574-6968.1994.tb06779.x

DO - 10.1111/j.1574-6968.1994.tb06779.x

M3 - Journal articles

AN - SCOPUS:85085672944

SN - 0378-1097

VL - 117

SP - 275

EP - 280

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 3

ER -