Open Accesscbb 3 ‐type cytochrome oxidase in the obligately chemolithoautotrophic Thiobacillus sp. W5
Author(s) -
Visser Jan M,
Jong Govardus A.H,
Vries Simon,
Robertson Lesley A,
Kuenen J.Gijs
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10231.x
Subject(s) - cytochrome c oxidase , heme , cytochrome , oxidase test , chemistry , heme a , thiobacillus , biochemistry , enzyme , organic chemistry , sulfur
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.