Inhibitiory effects of gold(III) ions on ribonuclease and deoxyribonuclease

Tatsuo Maruyama, Saori Sonokawa, Hironari Matsushita, Masahiro Goto

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    13 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)180-186
    Number of pages7
    JournalJournal of inorganic biochemistry
    Issue number1
    Publication statusPublished - Jan 2007

    All Science Journal Classification (ASJC) codes

    • Biochemistry
    • Inorganic Chemistry


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