Abstract
A highly active cytochrome c oxidase has been purified 75-fold from the neutrophilic obligately autotrophic Thiobacillus sp. W5. UV/visible and electron paramagnetic resonance spectroscopy revealed that the cytochrome c oxidase contains low-spin hemes c and low- and high-spin hemes b. HPLC analysis confirmed the presence of heme b as the sole type of non-covalently bound heme. The combined data from atomic absorption spectroscopy and electron paramagnetic resonance indicate the absence of Cu A and suggest the presence of a bimetallic heme-copper redox center. These results show that Thiobacillus sp. W5 contains a cbb 3-type oxidase, which is a member of the heme–copper oxidase family. The cbb 3-type oxidase was the only cytochrome oxidase expressed in aerobically and micro-aerobically grown Thiobacillus sp. W5 cultures.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
