The branched mitochondrial respiratory chain from Debaryomyces hansenii: Components and supramolecular organization
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چکیده
منابع مشابه
Lipids of Debaryomyces Hansenii.
Merdinger, Emanuel (Roosevelt University, Chicago, Ill.), and Edward M. Devine, Jr. Lipids of Debaryomyces hansenii. J. Bacteriol. 89:1488-1493. 1965.-The separation of neutral lipids and phospholipids from the lipid extract of Debaryomyces hansenii NRRL Y-1448 was accomplished by using a single column packed with silicic acid. The neutral lipids comprised 67%, and the phospholipids 33%, of the...
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We have isolated the cytosolic form of Cu-Zn superoxide dismutase (SOD) from the marine yeast Debaryomyces hansenii. This enzyme has a subunit mass of 18 kDa. The preparation was found to be heterogeneous by IF electrophoresis with two pI ranges: 5.14-4.0 and 1.6-1.8. The enzyme preparation had a remarkably strong stability at pH 6.0-7.0, surviving boiling for 10 min without losing more than 60...
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The existence of specific respiratory supercomplexes in mitochondria of most organisms has gained much momentum. However, its functional significance is still poorly understood. The availability of many deletion mutants in complex I (NADH:ubiquinone oxidoreductase) of Neurospora crassa, distinctly affected in the assembly process, offers unique opportunities to analyze the biogenesis of respira...
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Short-chain dehydrogenase reductases (SDRs) have been utilized for catalyzing the reduction of many aromatic/aliphatic prochiral ketones to their respective alcohols. However, there is a paucity of data that elucidates their innate biological role and diverse substrate space. In this study, we executed an in-depth biochemical characterization and substrate space mapping (with 278 prochiral keto...
متن کاملPurification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii.
A prolyl aminopeptidase (PAP) (EC 3.4.11.5) was isolated from the cell extract of Debaryomyces hansenii CECT12487. The enzyme was purified by selective fractionation with protamine and ammonium sulfate, followed by two chromatography steps, which included gel filtration and anion-exchange chromatography. The PAP was purified 248-fold, with a recovery yield of 1.4%. The enzyme was active in a br...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2014
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2013.07.011