Abstract
Cytochromec oxidase fromParacoccus denitrificans was homogenously dispersed in Triton X-100. Using gel exclusion chromatography and sucrose gradient centrifugation analysis a molecular weight of the detergent-protein complex of 155,000 was determined. After subtraction of the bound detergent (111 mol/mol hemeaa 3) a molecular weight of 85,000 resulted, which agreed well with the model of a monomer containing two subunits. This monomer showed high cytochromec oxidase activity when measured spectrophotometrically in the presence of Triton X-100 (V max=85 s−1). The molecular activity, plotted according to Eadie-Hofstee, was monophasic as a function of the cytochromec concentration. AK m of 3.6×10−6 M was evaluated, similar to theK m observed in the presence of dodecyl maltoside [Nałeczet al. (1985).Biochim. Biophys. Acta 808, 259–272].
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Bolli, R., Nałecz, K.A. & Azzi, A. Cytochromec oxidase fromParacoccus denitrificans in Triton X-100: Aggregation state and kinetics. J Bioenerg Biomembr 18, 277–284 (1986). https://doi.org/10.1007/BF00743048
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DOI: https://doi.org/10.1007/BF00743048