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Purification and properties of NADH dehydrogenase from a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius.
J Biochem 1987; 102(2):255-62JB

Abstract

An NADH dehydrogenase was purified to electrophoretical homogeneity from Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium optimally growing at pH 2-3 and 75 degrees 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.

Authors+Show Affiliations

Department of Life Science, Tokyo Institute of Technology, Kanagawa.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

2822684

Citation

Wakao, H, et al. "Purification and Properties of NADH Dehydrogenase From a Thermoacidophilic Archaebacterium, Sulfolobus Acidocaldarius." Journal of Biochemistry, vol. 102, no. 2, 1987, pp. 255-62.
Wakao H, Wakagi T, Oshima T. Purification and properties of NADH dehydrogenase from a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius. J Biochem. 1987;102(2):255-62.
Wakao, H., Wakagi, T., & Oshima, T. (1987). Purification and properties of NADH dehydrogenase from a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius. Journal of Biochemistry, 102(2), pp. 255-62.
Wakao H, Wakagi T, Oshima T. Purification and Properties of NADH Dehydrogenase From a Thermoacidophilic Archaebacterium, Sulfolobus Acidocaldarius. J Biochem. 1987;102(2):255-62. PubMed PMID: 2822684.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and properties of NADH dehydrogenase from a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius. AU - Wakao,H, AU - Wakagi,T, AU - Oshima,T, PY - 1987/8/1/pubmed PY - 1987/8/1/medline PY - 1987/8/1/entrez SP - 255 EP - 62 JF - Journal of biochemistry JO - J. Biochem. VL - 102 IS - 2 N2 - An NADH dehydrogenase was purified to electrophoretical homogeneity from Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium optimally growing at pH 2-3 and 75 degrees 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. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/2822684/Purification_and_properties_of_NADH_dehydrogenase_from_a_thermoacidophilic_archaebacterium_Sulfolobus_acidocaldarius_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/102.255?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -