Effect of periplasmic nitrate reductase on diauxic lag of Paracoccus pantotrophus
β Scribed by Kiranmai Durvasula; Kaemwich Jantama; Kyle Fischer; Adrian Vega; Ben Koopman; Spyros A. Svoronos
- Book ID
- 101761735
- Publisher
- American Institute of Chemical Engineers
- Year
- 2009
- Tongue
- English
- Weight
- 263 KB
- Volume
- 25
- Category
- Article
- ISSN
- 8756-7938
- DOI
- 10.1002/btpr.176
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## Abstract The catalytic mechanism of nitrate reduction by periplasmic nitrate reductases has been investigated using theoretical and computational means. We have found that the nitrate molecule binds to the active site with the Mo ion in the +6 oxidation state. Electron transfer to the active sit
Added vanadate ions inhibit purified nitrate reductase from Chlorella vulgar& by reacting with the enzyme in a manner rather similar to that of HCN. Thus vanadate, like HCN, forms an inactive complex with the reduced enzyme, and this inactivated enzyme can be reactivated rapidly by adding ferricyani