Skip to main content

Part of the book series: Aspects of Inorganic Chemistry

  • 175 Accesses

Abstract

Knowledge of the ligand environment of molybdenum in its enzymes is, to say the least, scanty. Such evidence as there is, based on comparisons between the e.p.r. parameters of, for example, xanthine oxidase and molybdenum complexes of sulphur ligands (see table 23, page 216), is thought to indicate molybdenum-sulphur binding. Most attention has been concentrated on cysteine as the obvious candidate for the role of a sulphur-containing biological ligand. Interest has also been shown in the potential alternative binding site for molybdenum, namely a flavin moiety, on the grounds that several of the molybdenum enzymes are metaloflavoproteins.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 34.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 44.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Similar content being viewed by others

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Copyright information

© 1975 Palgrave Macmillan, a division of Macmillan Publishers Limited

About this chapter

Cite this chapter

Mcauliffe, C.A. (1975). Model Studies. In: McAuliffe, C.A. (eds) Techniques and Topics in Bioinorganic Chemistry. Aspects of Inorganic Chemistry. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-02253-3_15

Download citation

Publish with us

Policies and ethics