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PMID: 6244539 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Fee JA, Choc MG, Findling KL, Lorence R, Yoshida T

Abstract

From the plasma membrane of Thermus thermophilus HB8 we have partially purified a detergent-solubilized complex of cytochromes a and c1 that actively catalyzes the transfer of electrons from ascorbate via a redox dye to oxygen. The complex is composed of two types of polypeptides, with molecular weights of approximately 55,000 and 33,000. Quantitative analysis revealed the presence of heme a, heme c, and copper in a ratio of 2:1:2, with the heme a being present at 10 +/- 1.3 nmol/mg of protein. The heme c was shown to be associated with the molecular weight 33,000 peptide and is suggested to be of the c1 type. The optical and electron paramagnetic resonance properties of this complex were found to be similar to those of eukaryotic cytochrome oxidase, suggesting the following arrangement of chromophores: a magnetically isolated cytochrome c1 and an oxygen-reducing functional unit consisting of two heme a groups and two copper ions associated with one or more larger peptides.

MeSH Terms
Copper/analysis Cytochromes/analysis,metabolism Electron Spin Resonance Spectroscopy Heme/analysis Hot Temperature Iron/analysis Isoelectric Focusing Molecular Weight Oxygen Consumption Thermodynamics Thermus/enzymology
Chemicals
Cytochromes Heme Copper Iron
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Fee J A
Choc M G
Findling K L
Lorence R
Yoshida T
References (33)
33 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1980-01-00
Pages
147-51
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC348225
Subset
IM
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