Xanthine oxidase catalyzed oxidation of aldehydes Oxidation of aliphatic aldehydes and 2- and 4-pyridinecarboxaldehyde
Gregory, D; Goodman, PA; Meany, JE
| HERO ID | 7132 |
|---|---|
| In Press | No |
| Year | 1972 |
| Title | Xanthine oxidase catalyzed oxidation of aldehydes Oxidation of aliphatic aldehydes and 2- and 4-pyridinecarboxaldehyde |
| Authors | Gregory, D; Goodman, PA; Meany, JE |
| Journal | Biochemistry |
| Volume | 11 |
| Issue | 24 |
| Page Numbers | 4472-4477 |
| Abstract | The xanthine oxidase catalyzed oxidations of a series of aliphatic aldehydes and 2- and 4-pyridinecarboxaldehydes were studied in phosphate buffers by monitoring the reduction of ferricytochrome c at 25.0° In aqueous solutions, these aldehydes exist in equilibrium with their hydrated forms. In order to clearly establish the relationship between the acid-base-catalyzed hydration of the aldehydes and the enzymatically catalyzed oxidation of the aldehyde-hydrate system, detailed kinetic analyses of both processes were carried out separately. Enzymatic catalysis was studied as a function of pH and of acetaldehyde concentration, and the catalytic components associated with the acid-base-catalyzed hydration of acetaldehyde in phosphate buffers were evaluated. These data, taken together, show not only that the unhydrated aldehyde is the substrate for xanthine oxidase action but also suggest that substantial enzymatic inhibition arises from the formation of the hydrate. The involvement of the unhydrated aldehyde as the preferential substrate is commnn for the aldehydes studied and in the evaluation of their respective Michaelis constants, Km: acetaldehyde, 0.0058 m; propionaldehyde, 0.014 μ; n-butyraldehyde, 0.048 m; 2-pyridinecarboxaldehyde, 0.0061 m; and 4-pyridinecarboxaldehyde, 0.002 m; correction was made to compensate for respective fractions of hydration. © 1972, American Chemical Society. All rights reserved. |
| Doi | 10.1021/bi00774a008 |
| Pmid | 4347179 |
| Wosid | WOS:A1972O008500008 |
| Url | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015519047&doi=10.1021%2fbi00774a008&partnerID=40&md5=dec4046e67da5228752bdab916a1d4b9 |
| Is Certified Translation | No |
| Dupe Override | No |
| Comments | Biochemistry 11: 4472-4477. |
| Is Public | Yes |
| Language Text | English |
| Is Qa | No |