Mechanism of reaction of fatty acid hydroperoxides with soybean peroxygenase.
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 268, Issue: 3, Page: 1708-1715
1993
- 34Citations
- 18Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations34
- Citation Indexes34
- CrossRef34
- Captures18
- Readers18
- 18
Abstract Description
13(S)-Hydroperoxyoctadeca-9(Z),11(E),15(Z)-trienoic acid (13-HPOT) was used to probe the mechanism of the hydroperoxide O-O bond cleavage catalyzed by solubilized and partially purified soybean peroxygenase. When reacted with this ferrihemoprotein, it was converted to 13(S)-hydroxyoctadeca-9(Z),11(E), 15(Z)-trienoic acid (13-HOT) and a single epoxide regio-isomer, i.e. 15,16-cis-epoxy-13(S)-hydroxyoctadeca-9(Z),11(E)-dienoic acid (15,16-EHOD). In the absence of co-oxidizable substrates, such as oleic acid or thiobenzamide, this latter compound accounted for about two-thirds of the reaction products. 13-HOT and 15,16-EHOD are products of heterolytic scission of the O-O bond of 13-HPOT; no products arising by homolytic scission could be detected. Therefore, soybean peroxygenase catalyzes hydroperoxide reduction exclusively by a heterolytic mechanism leading to a ferryl-oxo complex analogous to peroxidase compound I. In similar experiments, 13(S)-hydroperoxyoctadeca-9(Z),11(E)-dienoic acid gave 13(S)-hydroxyoctadeca-9(Z),11(E)-dienoic acid and 9,10 epoxy-13(S)-hydroxyoctadec-11(E)-enoic acid. Experiments with 18O-labeled 13-HPOT indicated that about 83% of the oxygen atom incorporated into the epoxide group of 15,16-EHOD, originated from the hydroperoxide group. Moreover, using mixtures of unlabeled and 18O-labeled 13-HPOT, it was established that this transfer takes place predominantly (about 3:1) by an intramolecular process. In the intermolecular reaction 13-HOT, formed after reduction of the hydroperoxide, diffuses from the active site and, after reassociation, is epoxidized at the 15,16-double bond. A unifying mechanistic scheme, which takes into account all of the reactions catalyzed by the peroxygenase, is proposed.
Bibliographic Details
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know