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A circular dichroism study of mitochondrial transhydrogenase from beef heart
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- Persson, Bengt L. (author)
- Department of Biochemistry and Biotechnology, Royal Institute of Technology
- Rydström, J (author)
- Kubista, M (author)
- (creator_code:org_t)
- 1991
- 1991
- English.
- In: Biophysical Chemistry. - 0301-4622 .- 1873-4200. ; 39:3, s. 267-272
- Journal article (peer-reviewed)
Abstract
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- This paper describes a circular dichroism (CD) spectroscopy study of purified proton-pumping nicotinamide nucleotide transhydrogenase from beef heart. The CD spectrum obtained was used to estimate the content of secondary structures of the purified enzyme and suggests the presence of 40–45% α-helical structure and long, possibly membrane-spanning α-helices. The spectrum was essentially unaffected by the absence or presence of transhydrogenase substrates, suggesting that the catalytic and proton-translocating activities of the enzyme occur without major rearrangements at the level of secondary structures.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Biochemistry
- Biokemi
- Biochemistry
- Biokemi
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- ref (subject category)
- art (subject category)
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