Inactivation of succinate dehydrogenase by 3-nitropropionate.
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چکیده
منابع مشابه
Inactivation of succinate dehydrogenase by 3-nitropropionate.
This paper examines proposals in the literature that 3-nitropropionate is a suicide inactivator of succinate dehydrogenase and that it acts by nucleophilic addition to N-5 of the covalently bound flavin component of the enzyme. With purified, soluble preparations of the enzyme, the inhibition developed slowly, and nearly complete inactivation occurred with a stoichiometric amount of 3-nitroprop...
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Since the experiments of KEARNEY 1 it has been known that both particle-bound and soluble succinate dehydrogenase can be activated by its substrate succinate and by competitive inhibitors such as fumarate, malonate and phosphate. Binding at the active centre apparently brings the enzyme in an active conformation. GUTMAN et al. 2) 3 have recently reported that NADH is as effective as succinate i...
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1. Succinate dehydrogenase flavocoenzyme (“SD-flavin”), previously shown to be an SOLsubstituted riboflavin derivative containing a tertiary nitrogen homoconjugated to the flavin nucleus, was subjected to further hydrolysis and to reduction under acid conditions. Both conditions resulted in the liberation of 1 mole of histidine per mole of flavin. This proves histidine to be the covalent link b...
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Reports in the literature have indicated that the fumarate reductase activity of succinate dehydrogenase, as measured by the fumarate-FMNHz assay, is not influenced by the state of activation of the enzyme. This conclusion was based on the observation that the activity in the fumarate reductase assay, measured at 19, where significant activation by succinate or malonate is not observed, was the...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50574-3