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The major soluble cytochromes of the obligately aerobic sulfur bacterium, Thiobacillus neapolitanus

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Abstract

Four cytochromes were isolated from soluble extracts of the aerobic sulfur bacterium, Thiobacillus neapolitanus. The two most abundant proteins were purified to homogeneity and thoroughly characterized. Cytochrome c-554 (547) is a monomeric, small molecular weight protein which is unusual in having two well-resolved alpha peaks in UV-visible absorption spectra. The redox potential is 208 mV. Native cytochrome c-549 is oligometric, but has a subunit size of about 26.000. The yield of this protein could be improved dramatically by washing membranes with 30% ammonium sulfate, but the material solubilized by this method had a larger native molecular weight than that in the initial 0.1 M Tris-Cl extract and behaved differently on chromatography. The properties of cytochrome c-549 including subunit size and UV-visible absorption spectra are similar to mitochondrial cytochrome c 1 and chloroplast cytochrome f, which suggests that it may be a modified form of the predominant membrane cytochrome. Based on cytochrome content, it is suggested that T. neapolitanus is not closely related to other thiobacilli.

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Dedicated to Prof. Dr. G. Drews on the occasion of his sixtieth birthday

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Trudinger, P.A., Meyer, T.E., Bartsch, R.G. et al. The major soluble cytochromes of the obligately aerobic sulfur bacterium, Thiobacillus neapolitanus . Arch. Microbiol. 141, 273–278 (1985). https://doi.org/10.1007/BF00428836

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  • DOI: https://doi.org/10.1007/BF00428836

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