Cytochrome aa3 from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

S. Anemüller; G. Schäfer

doi:10.1016/0014-5793(89)80581-2

Cytochrome aa₃ from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

S. Anemüller^*, G. Schäfer

^*Corresponding author for this work

Institute of Biochemistry

42 Citations (Scopus)

Abstract

Cytochrome aa₃ serves as a terminal oxidase in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. A procedure for its isolation is described. The purified preparation consists of only one major polypeptide of 38 kDa apparent molecular mass. The enzyme contains two heme α molecules with midpoint potentials of + 220 and + 370 mV, respectively. The copper content is at least 2 Cu/aa₃. It has only negligible capacity to oxidize cytochrome c, but rather serves as an oxidase for reduced caldariella quinone as present in the membrane of Sulfolobus.

Original language	English
Journal	FEBS Letters
Volume	244
Issue number	2
Pages (from-to)	451-455
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(89)80581-2
Publication status	Published - 27.02.1989

Funding

AcknowledgementTs:h e authors thank Mrs A. Lassen for skillful technicaal ssistancaen dMrs J. Kasperf or preparingth e drawings. This work was supportedi n part by Fonds der ChemischenIn dustrie.

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

10.1016/0014-5793(89)80581-2

Cite this

@article{f0a20e30d5934de3a744373e2a5e217f,

title = "Cytochrome aa3 from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius",

abstract = "Cytochrome aa3 serves as a terminal oxidase in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. A procedure for its isolation is described. The purified preparation consists of only one major polypeptide of 38 kDa apparent molecular mass. The enzyme contains two heme α molecules with midpoint potentials of + 220 and + 370 mV, respectively. The copper content is at least 2 Cu/aa3. It has only negligible capacity to oxidize cytochrome c, but rather serves as an oxidase for reduced caldariella quinone as present in the membrane of Sulfolobus.",

author = "S. Anem{\"u}ller and G. Sch{\"a}fer",

note = "Funding Information: AcknowledgementTs:h e authors thank Mrs A. Lassen for skillful technicaal ssistancaen dMrs J. Kasperf or preparingth e drawings. This work was supportedi n part by Fonds der ChemischenIn dustrie. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1989",

month = feb,

day = "27",

doi = "10.1016/0014-5793(89)80581-2",

language = "English",

volume = "244",

pages = "451--455",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc",

number = "2",

}

TY - JOUR

T1 - Cytochrome aa3 from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

AU - Anemüller, S.

AU - Schäfer, G.

N1 - Funding Information: AcknowledgementTs:h e authors thank Mrs A. Lassen for skillful technicaal ssistancaen dMrs J. Kasperf or preparingth e drawings. This work was supportedi n part by Fonds der ChemischenIn dustrie. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1989/2/27

Y1 - 1989/2/27

N2 - Cytochrome aa3 serves as a terminal oxidase in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. A procedure for its isolation is described. The purified preparation consists of only one major polypeptide of 38 kDa apparent molecular mass. The enzyme contains two heme α molecules with midpoint potentials of + 220 and + 370 mV, respectively. The copper content is at least 2 Cu/aa3. It has only negligible capacity to oxidize cytochrome c, but rather serves as an oxidase for reduced caldariella quinone as present in the membrane of Sulfolobus.

AB - Cytochrome aa3 serves as a terminal oxidase in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. A procedure for its isolation is described. The purified preparation consists of only one major polypeptide of 38 kDa apparent molecular mass. The enzyme contains two heme α molecules with midpoint potentials of + 220 and + 370 mV, respectively. The copper content is at least 2 Cu/aa3. It has only negligible capacity to oxidize cytochrome c, but rather serves as an oxidase for reduced caldariella quinone as present in the membrane of Sulfolobus.

UR - https://www.scopus.com/pages/publications/0011877563

U2 - 10.1016/0014-5793(89)80581-2

DO - 10.1016/0014-5793(89)80581-2

M3 - Journal articles

AN - SCOPUS:0011877563

SN - 0014-5793

VL - 244

SP - 451

EP - 455

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -