Coupling of dihydroriboflavin oxidation to the formation of the higher valence states of hemeproteins
dc.contributor.author | Feng, Xu | en_US |
dc.contributor.author | Hultquist, Donald E. | en_US |
dc.date.accessioned | 2006-04-10T14:30:33Z | |
dc.date.available | 2006-04-10T14:30:33Z | |
dc.date.issued | 1991-11-27 | en_US |
dc.identifier.citation | Feng, Xu, Hultquist, Donald E. (1991/11/27)."Coupling of dihydroriboflavin oxidation to the formation of the higher valence states of hemeproteins." Biochemical and Biophysical Research Communications 181(1): 197-203. <http://hdl.handle.net/2027.42/29022> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-4FW08RV-BM/2/b6a9a4ccca48696c02fbc911d2913a7c | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/29022 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1659807&dopt=citation | en_US |
dc.description.abstract | SummaryThe reactions between hydrogen peroxide and hemeproteins have been coupled to the oxidation of dihydroriboflavin so as to provide a simple method for measuring the rate constant of hemeprotein peroxidation. Dihydroriboflavin rapidly reduces the higher oxidation states of iron and the hydroxy radicals which are the products of the hemeprotein / hydrogen peroxide reaction. The rapid reduction of these highly reactive compounds prevents the hemeproteins from undergoing irreversible chemical modifications and thus allows the kinetics of peroxidation to be studied. The rate constants at pH 7.2 and 23[deg]C for the peroxidation of horseradish peroxidase, myoglobin, and ferrocytochrome c are found to be 6.2 x 106, 7.5 x 104, and 8 x 103M-1s-1, respectively. These studies suggest that reduced riboflavin might efficiently protect cells from oxidative damage such as that occurring in inflammation and reperfusion injury. | en_US |
dc.format.extent | 441589 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 | Coupling of dihydroriboflavin oxidation to the formation of the higher valence states of hemeproteins | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry Medical School, University of Michigan Ann Arbor, Michigan 48109-0606, USA. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry Medical School, University of Michigan Ann Arbor, Michigan 48109-0606, USA. | en_US |
dc.identifier.pmid | 1659807 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/29022/1/0000052.pdf | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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