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Acta Crystallographica. Section D, Biological Crystallography|August 16, 2000
Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coliJ Abramson, G Larsson, B Byrne, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 20, 1996
Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone moleculeA Puustinen, M I Verkhovsky, J E Morgan, et al.
Food Chemistry|January 12, 2015
Proteomic identification of allergenic seed proteins, napin and cruciferin, from cold-pressed rapeseed oilsT J Puumalainen, A Puustinen, S Poikonen, et al.
FEBS Letters|October 7, 1997
Bound water in the proton translocation mechanism of the haem-copper oxidasesS Riistama, G Hummer, A Puustinen, et al.
Biochemistry|October 27, 1992
The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme typeA Puustinen, J E Morgan, M Verkhovsky, et al.
FEBS Letters|May 30, 2001
Heme-copper oxidases with modified D- and K-pathways are yet efficient proton pumpsC M Gomes, C Backgren, M Teixeira, et al.
Nature Structural Biology|October 4, 2000
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding siteJ Abramson, S Riistama, G Larsson, et al.
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