Sulfhydryl-directed triggering of conformational changes in the enzyme rhodanese.
نویسندگان
چکیده
منابع مشابه
Acid pH-induced conformational changes in bovine liver rhodanese.
The enzyme rhodanese is greatly stabilized in the range pH 4-6, and samples at pH 5 are fully active after several days at 23 degrees C. This is very different from results at pH greater than 7, where there is significant loss of activity within 1 h. A pH-dependent conformational change occurs below pH 4 in a transition centered around pH 3.25 that leads slowly to inactive rhodanese at pH 3 (t ...
متن کاملConformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents.
Rhodanese is oxidatively inactivated by several reagents, some of which are not normally considered oxidants. Rhodanese, in a form not containing persulfide sulfur (E), was inactivated by phenylglyoxal under conditions where disulfides are formed. There was the concomitant increase in the fluorescence of the apolar probe 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid (bisANS). At 0.2 mg/ml ...
متن کاملBiochemical properties and biological functions of the enzyme rhodanese in domestic animals
The enzyme rhodanese (thiosulfate: cyanide sulfurtransferase) is a ubiquitous enzyme and its activity ispresent in all living organisms. Many functions including cyanide detoxification, formation of iron-sulfurcenters and participation in energy metabolism have been attributed to this enzyme. The enzyme catalyzesthe transfer of a sulfur atom from sulfane containing compounds (such as thiosulfat...
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15 صفحه اولFunctional roles of slow enzyme conformational changes in network dynamics.
Extensive studies from different fields reveal that many macromolecules, especially enzymes, show slow transitions among different conformations. This phenomenon is named such things as dynamic disorder, heterogeneity, hysteretic or mnemonic enzymes across these different fields, and has been directly demonstrated by single molecule enzymology and NMR studies recently. We analyzed enzyme slow c...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)81511-9