Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
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چکیده
منابع مشابه
Crystal structure and mechanism of action of the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas.
The crystal structure of the aldehyde oxidoreductase (Mop) from the sulphate-reducing bacterium Destdjovibrio gigas has been analysed and refined to 1.8A (0.18 nm) resolution in its native ‘desulpho’ form, as well as in ‘resulphurated’, oxidized, reduced and alcohol-bound forms [1,2], allowing a detailed look at several structural aspects relevant to catalysis. In analogy with eukaryotic xanthi...
متن کاملHydrogen evolution and consumption in AOT–isooctane reverse micelles by Desulfovibrio gigas hydrogenase
The enzyme hydrogenase isolated from the sulphate reducing anaerobic bacterium Desulfovibrio gigas was encapsulated in reverse micelles of AOT–water–isooctane. The enzyme ability to consume molecular hydrogen was studied as a function of the micelle size (given by Wo = [H2O]/[organic solvent]). A peak of catalytic activity was obtained for Wo = 18, a micelle size theoretically fitting the heter...
متن کاملKinetic and Structural Studies of Aldehyde Oxidoreductase from Desulfovibrio gigas Reveal a Dithiolene-Based Chemistry for Enzyme Activation and Inhibition by H2O2
Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and heterocyclic compounds. The molybdenum active site shows a distorted square-pyramidal geometry in which two ligands, a hydroxyl/water molecule (the catalytic labile site) and a sulfido ligand, have been shown to be essential for catalysis. The XO family member aldehyde oxi...
متن کاملOctomeric pyruvate-ferredoxin oxidoreductase from Desulfovibrio vulgaris.
Pyruvate-ferredoxin oxidoreductatse (PFOR) carries out the central step in oxidative decarboxylation of pyruvate to acetyl-CoA. We have purified this enzyme from Desulfovibrio vulgaris Hildenborough (DvH) as part of a systematic characterization of as many multiprotein complexes as possible for this organism, and the three-dimensional structure of this enzyme has been determined by a combinatio...
متن کاملDinitrophenol-stimulated adenosine triphosphatase activity in extracts of Desulfovibrio gigas.
A dinitrophenol (DNP)-stimulated adenosine triphosphatase (ATPase) has been found in both the soluble and particulate fractions of the anaerobic sulfate-reducing bacterium, Desulfovibrio gigas. As the soluble ATPase was labile to storage, only the particulate enzyme was studied in detail. It was optimally stimulated by DNP at 4 mm, and activity was insensitive to inhibition by ouabain. The ATPa...
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ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2003
ISSN: 0006-291X
DOI: 10.1016/s0006-291x(03)01337-8