Natta TansilaKristian BeckerChartchalerm Isarankura Na-AyudhyaVirapong PrachayasittikulLeif BülowMahidol UniversityLunds Universitet2018-07-122018-07-122008-08-01Biotechnology Letters. Vol.30, No.8 (2008), 1391-139615736776014154922-s2.0-45849152604https://repository.li.mahidol.ac.th/handle/20.500.14594/18879Green fluorescent protein (GFP) is frequently utilized for metal ion detection and quantification. To improve the metal binding potential of GFP, three residues (N146, F165, and L201) were substituted to histidines. Each variant responded differently upon interaction with metal ions. More than 80% of N146H, having the most accessible surface area, could bind to immobilized metal ions. However, only F165H exhibited significant differences in quenching by soluble metal ions (22% fluorescence decrease) in comparison with the template protein (12%). These findings can be utilized for designing GFP variants for metal binding and sensor applications. © 2008 Springer Science+Business Media B.V.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1007/s10529-008-9692-7