Title : Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity.

Pub. Date : 2005 Mar 22

PMID : 15766257






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 IscU functions as a scaffold for Fe-S cluster assembly and transfer, and is known to be a substrate protein for molecular chaperones. Iron iron-sulfur cluster assembly enzyme Homo sapiens
2 Kinetic studies of Fe-S cluster transfer from holo IscU to apo Fd in the presence of chaperone DnaK demonstrate an inhibitory effect on the rate of Fe-S cluster transfer from IscU. Iron iron-sulfur cluster assembly enzyme Homo sapiens
3 Kinetic studies of Fe-S cluster transfer from holo IscU to apo Fd in the presence of chaperone DnaK demonstrate an inhibitory effect on the rate of Fe-S cluster transfer from IscU. Iron iron-sulfur cluster assembly enzyme Homo sapiens
4 Kinetic studies of Fe-S cluster transfer from holo IscU to apo Fd in the presence of chaperone DnaK demonstrate an inhibitory effect on the rate of Fe-S cluster transfer from IscU. Iron iron-sulfur cluster assembly enzyme Homo sapiens
5 Kinetic studies of Fe-S cluster transfer from holo IscU to apo Fd in the presence of chaperone DnaK demonstrate an inhibitory effect on the rate of Fe-S cluster transfer from IscU. Iron iron-sulfur cluster assembly enzyme Homo sapiens
6 Rather, DnaK has a modest influence on the stability of the IscU-bound Fe-S cluster that may reflect a more important role in promoting cluster assembly. Iron iron-sulfur cluster assembly enzyme Homo sapiens