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

Publication ,  Journal Article
Hilton, JC; Rajagopalan, KV
Published in: Arch Biochem Biophys
January 1, 1996

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.

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Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

January 1, 1996

Volume

325

Issue

1

Start / End Page

139 / 143

Location

United States

Related Subject Headings

  • Rhodobacter sphaeroides
  • Pterins
  • Phosphates
  • Oxidoreductases
  • Molybdenum
  • Molecular Structure
  • Iron-Sulfur Proteins
  • Guanine Nucleotides
  • Guanine
  • Biochemistry & Molecular Biology
 

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Journal cover image

Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

January 1, 1996

Volume

325

Issue

1

Start / End Page

139 / 143

Location

United States

Related Subject Headings

  • Rhodobacter sphaeroides
  • Pterins
  • Phosphates
  • Oxidoreductases
  • Molybdenum
  • Molecular Structure
  • Iron-Sulfur Proteins
  • Guanine Nucleotides
  • Guanine
  • Biochemistry & Molecular Biology