Cadmium and arsenite binding by N-dihydrolipoyl-aminoethoxydextran: A model study of enzyme dithiol criteria
dc.contributor.author | Gaber, Bruce P. | en_US |
dc.contributor.author | Fluharty, Arvan L. | en_US |
dc.date.accessioned | 2006-04-17T16:43:22Z | |
dc.date.available | 2006-04-17T16:43:22Z | |
dc.date.issued | 1973 | en_US |
dc.identifier.citation | Gaber, Bruce P., Fluharty, Arvan L. (1973)."Cadmium and arsenite binding by N-dihydrolipoyl-aminoethoxydextran: A model study of enzyme dithiol criteria." Bioinorganic Chemistry 2(2): 135-148. <http://hdl.handle.net/2027.42/33970> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6W7Y-4344CXG-3/2/c4aa0aaf6ceeb891a9369220cd60e2e5 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/33970 | |
dc.description.abstract | We have observed the interaction of Cd2+, Zn2+, and AsO22- with a dithiol-substituted polymer (N-dihydrolipoyl aminoethoxy dextran). Cadmium binding results in an intense uv difference spectrum ([lambda]max = 240 nm). Spectrophotometric titrations with CdCl2 reveal formation of two Cd-dithiol complexes characterized as 2--SH/Cd2+ and 3--SH/Cd2+. Stability constants were determined by titration of cadmium-saturated polymer with excess EDTA. For the two complexes, K1 = 2.7 x 1014 M and K2 = 7.7 x 1013 M. NTA is not effective in displacing Cd2+. In competition of Cd2+ and Zn2+ for dithiol sites, Cd2+ is bound about 500 times more firmly than Zn2+. Arsenite binding is sluggish (K ~ 85 M-1 sec-1) and yields a single complex (2--SH/AsO22-). Competition and kinetic data suggest that 106 M KAsO2- 2 M. We have defined basic criteria for evaluation of enzyme active-site dithiols: (1) the binding order "cadmium stronger than zinc"; (2) relief of Cd2+ inhibition by 10-fold excess EDTA and no relief by 10-fold excess of NTA; (3) inhibition by arsenite. | en_US |
dc.format.extent | 990721 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Cadmium and arsenite binding by N-dihydrolipoyl-aminoethoxydextran: A model study of enzyme dithiol criteria | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Natural Sciences, University of Michigan Dearborn, Dearborn, Michigan, 48128 USA | en_US |
dc.contributor.affiliationother | Research Department, Pacific State Hospital, Pomona, California 91768 USA | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/33970/1/0000242.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/S0006-3061(00)80157-X | en_US |
dc.identifier.source | Bioinorganic Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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