Subunit sites of oxidative inactivation of Escherichia coli F1-ATPase by HOCl.
Cellular inactivation of Escherichia coli by the neutrophil-generated toxin, hypochlorous acid, is accompanied by inactivation of its plasma membrane-localized F1-ATPase. The nature of oxidative damage leading to inactivation of this enzyme was probed by SDS-PAGE and 2D-gel electrophoresis and by hybrid reconstitution studies using purified subunits from untreated and extensively oxidized bacteria. The data indicate that inactivation is due to selective oxidation of a few highly vulnerable sites; although damage occurred to each of the alpha, beta, and gamma-subunits required for soluble ATP hydrolase activity, the extent of damage was insufficient to alter their electrophoretic properties.
Hannum
D M
DM
Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97006-1999, USA.
Barrette
W C
WC
Hurst
J K
JK
D001665:Binding Sites; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D006997:Hypochlorous Acid / Q000494:pharmacology*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000302:isolation & purification
D006997:Hypochlorous Acid; D006180:Proton-Translocating ATPases