Chen Y, Dey S, Rosen B P
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
J Bacteriol. 1996 Feb;178(3):911-3. doi: 10.1128/jb.178.3.911-913.1996.
The single cysteine in the ArsB protein subunit of the arsenite resistance pump was changed to serine and alanine residues. Resistance in cells expressing the two mutant arsB genes was the same as in the wild type, and the serine substitution had no effect on the arsenite transport properties. These results eliminate possible thiol chemistry in translocation. Thus, the pump uses soft metal chemistry for metalloactivation and nonmetal chemistry for oxyanion transport.
将抗砷泵的ArsB蛋白亚基中的单个半胱氨酸替换为丝氨酸和丙氨酸残基。表达这两个突变arsB基因的细胞中的抗性与野生型相同，丝氨酸替代对砷酸盐转运特性没有影响。这些结果排除了转运过程中可能存在的硫醇化学作用。因此，该泵利用软金属化学进行金属激活，利用非金属化学进行含氧阴离子转运。
