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• W2030576504 startingPage "308" @default.
• W2030576504 abstract "A soluble c ‐type cytochrome was purified to homogeneity from Thiobacillus ferrooxidans. This cytochrome is characterised by an α‐peak wavelength of 552 nm, a molecular mass of 21193 Da (as determined by mass spectroscopy), and a pI value of 9. N‐terminal sequencing yielded the polypeptide sequence up to the 50th residue. The iron content of 1.9 Fe/molecule and the heme/molecule ratio of 2.15 identified this cytochrome as a diheme protein. Optical redox titrations at pH 3.0 revealed the presence of two distinguishable redox species with E m = 385 mV±20 mV and E m = 480 mV±20 mV. EPR spectra recorded on this heme protein showed the presence of two distinct spectral species with g z = 3.1 and g z = 3.35. The g z = 3.35 heme corresponds to the higher potential redox species. In line with the differences in E m values, the two heme species were oxidised by O 2 with significantly differing half‐times. All the above mentioned properties demonstrate that this heme protein belongs to the c 4 family of diheme cytochromes. The characteristics and functional role of the studied heme protein are discussed with reference to other c ‐type cytochromes described in Thiobacilli . Its properties are furthermore compared to other members of the cytochrome c 4 family." @default.
• W2030576504 created "2016-06-24" @default.
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• W2030576504 date "1996-12-01" @default.
• W2030576504 modified "2023-10-03" @default.
• W2030576504 title "Characterisation of a Soluble Cytochrome c4 Isolated from Thiobacillus ferrooxidans" @default.
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• W2030576504 doi "https://doi.org/10.1111/j.1432-1033.1996.0308r.x" @default.
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