| Literature DB >> 2558649 |
T Wakagi1, T Yamauchi, T Oshima, M Müller, A Azzi, N Sone.
Abstract
Cytochrome C oxidase was solubilized with a nonionic detergent n-decanoyl-N-methyl glucamide from the membranes of Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium, and was purified. The enzyme oxidized horse heart cytochrome C with a Vmax of 63 mumols/min/mg at 50 degrees C. The activity was sensitive to cyanide. The enzyme also catalyzed oxygen uptake detergent on N, N, N', N'-tetramethyl p-phenylene diamine. An apparent molecular mass was estimated to be 150 kDa. The enzyme is composed of three subunits of 37, 23 and 14 kDa. Spectral characteristics were similar to typical bacterial aa3 except for the presence of a novel 583 nm peak observed in reduced minus oxidized difference spectrum.Entities:
Mesh:
Substances:
Year: 1989 PMID: 2558649 DOI: 10.1016/0006-291x(89)92717-4
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575