The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Purification and Properties of NADH Dehydrogenase from a Thermoacidophilic Archaebacterium, Sulfolobus acidocaldarius
Hiroshi WAKAOTakayoshi WAKAGITairo OSHIMA
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JOURNAL FREE ACCESS

1987 Volume 102 Issue 2 Pages 255-262

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Abstract

An NADH dehydrogenase was purified to electrophoretical homogeneity from Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium optimally growing at pH 2-3 and 75°C. A 2, 100-fold purification was achieved. The purified enzyme is an acidic protein with an isoelectric point of 5.6 and a molecular weight of 95, 000, consisting of two 50, 000-dalton subunits. The enzyme showed an absorption spectrum characteristic of flavoproteins, with maxima at 272, 372, and 448 nm. The enzyme is highly thermostable, is specific for NADH as an electron donor, and is capable of using 2, 6-dichlorophenolindophenol, ferricyanide, benzoquinone, and naphthoquinone as electron acceptors. Though at a low rate, caldariellaquinone, a unique and sole benzothiophenequinone in the genus Sulfolobus, was also reduced by the enzyme, suggesting that the enzyme is a possible member of the respiratory chain of the thermoacidophilic archaebacterium.

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© The Japanese Biochemical Society
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