Chromium (III) thiamin diphosphate: a new probe of enzyme coenzyme–metal ion binding. Interaction with wheat germ pyruvate decarboxylase
1978 ◽
Vol 56
(10)
◽
pp. 999-1001
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Keyword(s):
Chromium (III) thiamin diphosphate (CrTDP) is a substitutionally inert complex which is a physical and kinetic probe of the binding mode of metal ion and coenzyme in thiamin diphosphate (TDP) dependent enzymes. CrTDP is prepared by reaction of aquated Cr (III) and TDP and purified by ion-exchange chromatography. CrTDP binds to the apoenzyme of wheat germ pyruvate decarboxylase, giving an inactive holoenzyme. Chromium (III) ion binds to the apoenzyme in a manner that suggests, in light of the results with CrTDP, that there are two metal ion binding sites. Extension of the use of CrTDP to other enzymes can give specific information about binding and can introduce an active site reporter group.
Interaction of RNase A with VO3-and VO2+Ions. Metal Ion Binding Mode and Protein Secondary Structure
1999 ◽
Vol 17
(3)
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pp. 473-480
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Keyword(s):
Rnase A
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2004 ◽
Vol 69
(4)
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pp. 885-896
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Keyword(s):
Keyword(s):
1991 ◽
Vol 266
(11)
◽
pp. 7291-7299
1984 ◽
Vol 259
(2)
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pp. 903-908
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