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The carbon monoxide- and oxygen-reacting haemoproteins of Streptomyces clavuligerus : cytochrome aa 3 is the predominant terminal oxidase of the respiratory chain

The carbon monoxide- and oxygen-reacting haemoproteins of Streptomyces clavuligerus : cytochrome... 203 150 150 5 5 Robert I. Scott Robert K. Poole School of Biotechnology Polytechnic of Central London 115 New Cavendish Street W1M 8JS London UK Department of Microbiology Kings College London Kensington Campus, Campden Hill Road W8 7AH London UK Abstract The nature of the carbon monoxide- and oxygen-reacting haemoproteins in the respiratory chain of the filamentous antibiotic-producing bacterium Streptomyces clavuligerus has been investigated. CO-difference (i.e. CO+ reduced minus reduced) spectra of intact cells showed the presence of cytochrome aa 3 , a CO binding b -type cytochrome, and a pigment resembling cytochrome d . In addition, cells that were approaching the end of the growth phase showed the presence of cytochrome P450: this pigment was undetectable in cells harvested early in the growth cycle. High speed centrifugation of cell-free extracts prepared from cells broken by sonication showed that cytochrome aa 3 was tightly membrane-bound and that cytochrome P450 was soluble. Inhibition of oxygen uptake rates of cells by cyanide indicated that one component, which showed 50% inhibition at 2–4 mM CN − , was acting as major terminal oxidase: this was observed in cells harvested from all stages of growth. Photodissociation (i. e. photolysed, CO reduced minus CO reduced) spectra at-118°C, in the absence of oxygen, showed cytochrome aa 3 to be the sole photolysable CO-reacting haemoprotein. At higher temperature (-87°C), in the presence of oxygen, cytochrome aa 3 formed a complex with oxygen that could not be photolysed by similar intensities of light. By raising the temperature to-43°C, the oxidation of c -type cytochromes was observed. It is concluded that cytochrome aa 3 is the predominant terminal oxidase in S. clavuligerus and that the other CO reacting haemoproteins, of unknown function, are unlikely to be oxidases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

The carbon monoxide- and oxygen-reacting haemoproteins of Streptomyces clavuligerus : cytochrome aa 3 is the predominant terminal oxidase of the respiratory chain

Scott, Robert; Poole, Robert
Archives of Microbiology , Volume 150 (5) – Sep 1, 1988
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References (31)

Publisher
Springer Journals
Copyright
Copyright © 1988 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00422288
Publisher site
See Article on Publisher Site

Abstract

203 150 150 5 5 Robert I. Scott Robert K. Poole School of Biotechnology Polytechnic of Central London 115 New Cavendish Street W1M 8JS London UK Department of Microbiology Kings College London Kensington Campus, Campden Hill Road W8 7AH London UK Abstract The nature of the carbon monoxide- and oxygen-reacting haemoproteins in the respiratory chain of the filamentous antibiotic-producing bacterium Streptomyces clavuligerus has been investigated. CO-difference (i.e. CO+ reduced minus reduced) spectra of intact cells showed the presence of cytochrome aa 3 , a CO binding b -type cytochrome, and a pigment resembling cytochrome d . In addition, cells that were approaching the end of the growth phase showed the presence of cytochrome P450: this pigment was undetectable in cells harvested early in the growth cycle. High speed centrifugation of cell-free extracts prepared from cells broken by sonication showed that cytochrome aa 3 was tightly membrane-bound and that cytochrome P450 was soluble. Inhibition of oxygen uptake rates of cells by cyanide indicated that one component, which showed 50% inhibition at 2–4 mM CN − , was acting as major terminal oxidase: this was observed in cells harvested from all stages of growth. Photodissociation (i. e. photolysed, CO reduced minus CO reduced) spectra at-118°C, in the absence of oxygen, showed cytochrome aa 3 to be the sole photolysable CO-reacting haemoprotein. At higher temperature (-87°C), in the presence of oxygen, cytochrome aa 3 formed a complex with oxygen that could not be photolysed by similar intensities of light. By raising the temperature to-43°C, the oxidation of c -type cytochromes was observed. It is concluded that cytochrome aa 3 is the predominant terminal oxidase in S. clavuligerus and that the other CO reacting haemoproteins, of unknown function, are unlikely to be oxidases.

Journal

Archives of Microbiology – Springer Journals

Published: Sep 1, 1988

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