| scholarly article | Q13442814 |
| P356 | DOI | 10.1042/BJ2740723 |
| P953 | full work available at URL | https://europepmc.org/articles/PMC1149971 |
| https://europepmc.org/articles/PMC1149971?pdf=render | ||
| https://portlandpress.com/biochemj/article-pdf/274/3/723/604666/bj2740723.pdf | ||
| https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/1849404/?tool=EBI | ||
| https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/1849404/pdf/?tool=EBI | ||
| P932 | PMC publication ID | 1149971 |
| P698 | PubMed publication ID | 1849404 |
| P5875 | ResearchGate publication ID | 21307388 |
| P2093 | author name string | R. K. Poole | |
| I. Salmon | |||
| W. J. Ingledew | |||
| B. Bolgiano | |||
| P2860 | cites work | Structural models of the redox centres in cytochrome oxidase | Q24556092 |
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| Regulation of expression of the cytochrome d terminal oxidase in Escherichia coli is transcriptional | Q36189791 | ||
| Immunological investigation of the distribution of cytochromes related to the two terminal oxidases of Escherichia coli in other gram-negative bacteria | Q36290742 | ||
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| The identity of a new copper(II) electron paramagnetic resonance signal in cytochrome c oxidase | Q72885906 | ||
| A method for in situ characterization of b- and c-type cytochromes in Escherichia coli and in Complex III from beef heart mitochondria by combined spectrum deconvolution and potentiometric analysis | Q72949316 | ||
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| P407 | language of work or name | English | Q1860 |
| P921 | main subject | cell biology | Q7141 |
| biochemistry | Q7094 | ||
| Escherichia coli | Q25419 | ||
| P304 | page(s) | 723-730 | |
| P577 | publication date | 1991-03-01 | |
| 1991-03-15 | |||
| P1433 | published in | Biochemical Journal | Q864221 |
| P1476 | title | Redox analysis of the cytochrome o-type quinol oxidase complex of Escherichia coli reveals three redox components | |
| P478 | volume | 274 ( Pt 3) |
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| Q38755013 | Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases |
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