ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Cytochrome c oxidase from the novel alkaliphilic autotrophic sulfur bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 was isolated and purified 87-fold. Spectroscopic analysis revealed the presence of both c- and b-type hemes as well as copper in a ratio of 3:2:1. The purified enzyme consists of three subunits with apparent molecular masses of 41, 34 and 32 kDa. The two small subunits contain covalently bound heme c. With TMPD as a substrate the pH optimum was determined to be pH 8.0. In the presence of monovalent cations the specific activity of the purified oxidase increased significantly. The enzyme was not able to oxidize external cytochrome c, but accepted electron from its native electron donor. The latter was separated from the other membrane cytochromes during anion-exchange chromatography and was identified as a high potential cytochrome c551. Overall the data indicate that the cytochrome c oxidase from this alkaliphilic autotrophic bacterium belongs to the heme-copper oxidase superfamily; regarding its subunit composition and content of prosthetic groups, the enzyme is similar in many aspects to the cbb3-type cytochrome c oxidases described for several neutrophilic bacteria, including anaerobic phototrophic and aerobic sulfur-oxidizing bacteria.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1999.tb08713.x
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