Refine
Year of publication
Document Type
- Article (121)
- Postprint (14)
- Review (13)
- Conference Proceeding (3)
- Other (1)
Language
- English (152)
Is part of the Bibliography
- yes (152) (remove)
Keywords
- molybdenum cofactor (9)
- Molybdenum cofactor (7)
- Moco biosynthesis (4)
- Molybdenum (4)
- bis-MGD (4)
- persulfide (4)
- sulfite oxidase (4)
- Aldehyde oxidase (3)
- Aldehyde oxidoreductase (3)
- Bioelectrocatalysis (3)
The enzyme xanthine dehydrogenase (XDH) from the purple photosynthetic bacterium Rhodobacter capsulatus catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid as part of purine metabolism. The native electron acceptor is NAD(+) but herein we show that uric acid in its 2-electron oxidized form is able to act as an artificial electron acceptor from XDH in an electrochemically driven catalytic system. Hypoxanthine oxidation is also observed with the novel production of uric acid in a series of two consecutive 2-electron oxidation reactions via xanthine. XDH exhibits native activity in terms of its pH optimum and inhibition by allopurinol.
The TorD family of specific chaperones is divided into four subfamilies dedicated to molybdoenzyme biogenesis and a fifth one, exemplified by YcdY of Escherichia coli, for which no defined partner has been identified so far. We propose that YcdY is the chaperone of YcdX, a zinc protein involved in the swarming motility process of E. coli, since YcdY interacts with YcdX and increases its activity in vitro.