PMID- 22450312 OWN - NLM STAT- MEDLINE DCOM- 20120622 LR - 20120423 IS - 1090-2104 (Electronic) IS - 0006-291X (Linking) VI - 420 IP - 4 DP - 2012 Apr 20 TI - Study of the electrostatic effects of mutations on the surface of dehaloperoxidase-hemoglobin A. PG - 733-7 LID - 10.1016/j.bbrc.2012.03.053 [doi] AB - 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. CI - Copyright (c) 2012 Elsevier Inc. All rights reserved. FAU - Zhao, Junjie AU - Zhao J AD - Department of Chemistry, North Carolina State University, Raleigh, NC 27695, USA. FAU - Rowe, Jennifer AU - Rowe J FAU - Franzen, Jocelyn AU - Franzen J FAU - He, Chi AU - He C FAU - Franzen, Stefan AU - Franzen S LA - eng PT - Journal Article PT - Research Support, U.S. Gov't, Non-P.H.S. DEP - 20120317 PL - United States TA - Biochem Biophys Res Commun JT - Biochemical and biophysical research communications JID - 0372516 RN - 0 (Recombinant Proteins) RN - 9034-51-9 (Hemoglobin A) RN - EC 1.11.1.- (Peroxidases) SB - IM MH - Animals MH - Hemoglobin A/*chemistry/genetics MH - Mutagenesis MH - Mutation MH - Peroxidases/*chemistry/genetics MH - Polychaeta/*enzymology MH - Recombinant Proteins/chemistry/genetics MH - *Static Electricity EDAT- 2012/03/28 06:00 MHDA- 2012/06/23 06:00 CRDT- 2012/03/28 06:00 PHST- 2012/03/02 00:00 [received] PHST- 2012/03/12 00:00 [accepted] PHST- 2012/03/28 06:00 [entrez] PHST- 2012/03/28 06:00 [pubmed] PHST- 2012/06/23 06:00 [medline] AID - S0006-291X(12)00500-1 [pii] AID - 10.1016/j.bbrc.2012.03.053 [doi] PST - ppublish SO - Biochem Biophys Res Commun. 2012 Apr 20;420(4):733-7. doi: 10.1016/j.bbrc.2012.03.053. Epub 2012 Mar 17.