Beltramini M, Giacometti G M, Salvato B, Giacometti G, Münger K, Lerch K
Department of Biology, University of Padova, Italy.
Biochem J. 1989 May 15;260(1):189-93. doi: 10.1042/bj2600189.
The luminescence lifetime of Cu-metallothionein from the fungus Neurospora crassa has been studied by the frequency-domain emission technique. Lifetimes of 10.3 and 3.4 microseconds have been found for the protein in the absence and in the presence of oxygen respectively. Binding of Hg(II) results in a quenching of the luminescence correlated to the shortening of lifetime to 0.3-0.4 microsecond. No quenching by oxygen is found for the Hg(II)-Cu-metallothionein adduct. By analogy to model compounds, luminescence emission is attributed to a triplet excited state of a Cu(I)-to-sulphur charge-transfer complex. The comparison of bimolecular quenching constants for O2 and acrylamide indicates a highly compact structure of the protein.
利用频域发射技术研究了来自粗糙脉孢菌的铜金属硫蛋白的发光寿命。分别在无氧和有氧条件下测得该蛋白质的发光寿命为10.3微秒和3.4微秒。汞（II）的结合导致发光猝灭，寿命缩短至0.3 - 0.4微秒。汞（II）-铜金属硫蛋白加合物未发现被氧猝灭的情况。与模型化合物类似，发光发射归因于铜（I）到硫的电荷转移配合物的三重激发态。氧气和丙烯酰胺的双分子猝灭常数比较表明该蛋白质具有高度紧密的结构。
