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Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur‐oxidizing bacteria
Author(s) -
Sorokin Dimitry Yu,
de Jong Govardus A.H,
Robertson Lesley A,
Kuenen Gijs J
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00379-2
Subject(s) - chemistry , sulfide , oxidizing agent , enzyme , sulfur , biochemistry , cytochrome , heme , dehydrogenase , bacteria , oxidoreductase , organic chemistry , biology , genetics
Extracts of the alkaliphilic sulfur‐oxidizing autotroph strain AL3 contained sulfide:cytochrome c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X‐100 extraction, further purification resulted in an enzyme that catalyzed sulfide oxidation with horse heart cytochrome c . This enzyme was a 41 kDa protein containing heme c 554 . The optimum pH of the membrane bound enzyme was 9.0, but after extraction this fell to 8.0. The enzyme catalyzed a single electron oxidation of HS − . Hydrosulfide radical is therefore the most probable product.