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Title: Molybdenum center of xanthine dehydrogenase

Thesis/Dissertation ·
OSTI ID:5873200

Cyanolysis of native, oxidized xanthine dehydrogenase is known to inactivate the enzyme by removing a unique sulfur as thiocyanate. Chemical, genetic, and spectroscopic evidence indicates that this sulfur is a terminal ligand of Mo and is present in native xanthine dehydrogenase, but not in cyanolyzed xanthine dehydrogenase or native sulfite oxidase. A procedure for rapid, reproducible, and quantitative reconstitution of desulfo Mo hydroxylases with sulfide was developed. The cyanolyzable sulfur of xanthine dehydrogenase was specifically radiolabeled with /sup 35/sulfide using this procedure. Various chemical properties of the cyanolyzable sulfur could be determined with the radiolabelled enzyme. The data support the conclusion that the cyanolyzable sulfur is a terminal sulfur ligand of the Mo atoms, and is not part of an organic moiety. Application of the resulfuration procedure to crude extracts of Drosophila melanogaster ma-1 flies, which are pleiotropically deficient in xanthine dehydrogenase and aldehyde oxidase, led to the emergence of these enzyme activities. Evidence for the identity of in vitro reconstituted xanthine dehydrogenase from ma-1 mutants with wild type enzyme is presented. A system for efficient reconstitution of the apo-subunits of the molybdoenzyme nitrate reductase from the Neurospora crassa mutant nit-1 with molybdenum cofactor from denatured purified molybdoenzymes in the absence of exogenous molybdate was developed.

Research Organization:
Duke Univ., Durham, NC (USA)
OSTI ID:
5873200
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English