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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ferguson, Stuart J. De Vries, Simon Strampraad, Marc J. F. Sam, Katharine A. |
| Description | Author Affiliation: Sam KA ( Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.) |
| Abstract | Paracoccus pantotrophus cytochrome cd(1) is a nitrite reductase found in the periplasm of many denitrifying bacteria. It catalyzes the reduction of nitrite to nitric oxide during the denitrification part of the biological nitrogen cycle. Previous studies of early millisecond intermediates in the nitrite reduction reaction have shown, by comparison with pH 7.0, that at the optimum pH, approximately pH 6, the earliest intermediates were lost in the dead time of the instrument. Access to early time points (approximately 100 micros) through use of an ultra-rapid mixing device has identified a spectroscopically novel intermediate, assigned as the Michaelis complex, formed from reaction of fully reduced enzyme with nitrite. Spectroscopic observation of the subsequent transformation of this species has provided data that demand reappraisal of the general belief that the two subunits of the enzyme function independently. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 41 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-10-10 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cytochromes Chemistry Nitrite Reductases Nitrites Paracoccus Enzymology Periplasmic Proteins Hydrogen-Ion Concentration Oxidation-Reduction Time Factors Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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