Abstract:
: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 c554. 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sorokin DYu,de Jong GA,Robertson LA,Kuenen GJdoi
10.1016/s0014-5793(98)00379-2subject
Has Abstractpub_date
1998-05-01 00:00:00pages
11-4issue
1eissn
0014-5793issn
1873-3468pii
S0014579398003792journal_volume
427pub_type
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