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A circular dichroism study of mitochondrial transhydrogenase from beef heart
B Persson1, J Rydström, M Kubista
1Department of Biochemistry and Biotechnology, Royal Institute of Technology, Stockholm, Sweden.
Abstract:
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% alpha-helical structure and long, possibly membrane-spanning alpha-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.