Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria.

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 Lett

journal_title

FEBS letters

authors

Sorokin DYu,de Jong GA,Robertson LA,Kuenen GJ

doi

10.1016/s0014-5793(98)00379-2

subject

Has Abstract

pub_date

1998-05-01 00:00:00

pages

11-4

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014579398003792

journal_volume

427

pub_type

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