Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum.

Published

Journal Article

Chemical analysis of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans has shown that its molybdenum center contains two molybdopterin guanine dinucleotide molecules and a single atom of molybdenum. The enzyme, which exists as a monomer of 86 kDa, was shown to contain 1 mol of molybdenum, 4 mol of organic phosphate, and 2 mol of guanine per mole of protein. In addition, the relative yield of Form A, a fluorescent derivative of molybdopterin, was twice that obtained from sulfite oxidase, a protein which contains a single molybdopterin per molybdenum. These findings correlate with the recent report of the presence of two molybdopterin ligands in the tungsten cofactor of aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus, providing the first example of a bis(pterin)molybdenum cofactor and extending this structural motif to the molybdopterin dinucleotide enzymes.

Full Text

Duke Authors

Cited Authors

  • Hilton, JC; Rajagopalan, KV

Published Date

  • January 1, 1996

Published In

Volume / Issue

  • 325 / 1

Start / End Page

  • 139 - 143

PubMed ID

  • 8554338

Pubmed Central ID

  • 8554338

International Standard Serial Number (ISSN)

  • 0003-9861

Digital Object Identifier (DOI)

  • 10.1006/abbi.1996.0017

Language

  • eng

Conference Location

  • United States