@article{zhao_rowe_franzen_he_franzen_2012, title={Study of the electrostatic effects of mutations on the surface of dehaloperoxidase-hemoglobin A}, volume={420}, ISSN={["0006-291X"]}, DOI={10.1016/j.bbrc.2012.03.053}, abstractNote={Point mutations of dehaloperoxidase-hemoglobin A (DHP A) that affect the surface charge have been prepared to study the interaction between DHP A with its substrate 2,4,6-trichlorophenol (TCP). Kinetic studies of these surface mutations showed a correlation, in which the more positively charged mutants have increased catalytic efficiency compared with wild type DHP A. As a result, the hypothesis of this study is that there is a global electrostatic interaction between DHP A and TCP. The electrostatic nature of substrate binding was further confirmed by the result that kinetic assays of DHP A were affected by ionic strength. Furthermore, isoelectric focusing (IEF) gel study showed that the pI-6.8 for DHP A, which indicates that DHP A has a slight negative charge pH 7, consistent with the kinetic observations.}, number={4}, journal={BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS}, author={Zhao, Junjie and Rowe, Jennifer and Franzen, Jocelyn and He, Chi and Franzen, Stefan}, year={2012}, month={Apr}, pages={733–737} }