Abstract:
:Inhibitory effects of gold(III) ions (Au(III)) on ribonuclease A (RNase A) and deoxyribonuclease I (DNase I) were investigated at neutral pH. RNase A was completely inhibited by 3 molar equivalents of Au(III) ions. DNase I was inhibited by 10 molar equivalents of Au(III) ions. Stoichiometric analyses suggest that Au(III) ions were coordinated to RNase A molecules. The Au(III)-inhibited RNase A and DNase I were renatured to exhibit 80% and 60% of their intrinsic activity, when the bound Au(III) ions were eliminated from the nucleases by addition of thiourea, which forms a strong complex with gold ions. This suggests that RNase A and DNase I were not oxidized to lose their activity, but reversibly complexed with Au(III) ions to lose their activity. Au(III) ions were probably considered to be bound to histidine and methionine residues in the nucleases, resulting in the inhibition of their activity. CD spectra revealed that the Au(III)-induced inhibition caused a conformational change in RNase A molecules and that the addition of thiourea induced refolding of the Au(III)-inhibited RNase A.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Maruyama T,Sonokawa S,Matsushita H,Goto Mdoi
10.1016/j.jinorgbio.2006.09.021subject
Has Abstractpub_date
2007-01-01 00:00:00pages
180-6issue
1eissn
0162-0134issn
1873-3344pii
S0162-0134(06)00280-7journal_volume
101pub_type
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pub_type: 杂志文章
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journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
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更新日期:2006-03-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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