Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 22nd May 2019 from 11:00 AM to 1:00 PM (GMT).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.

All chapters
Previous chapter Next chapter


Electron Transfer Mechanisms in Molybdenum and Tungsten Model Compounds

This review briefly deals with the modelling of a diverse class of Mo and W enzymes based on the active site structure of the Mo (W)-co with ene-dithiolate coordination. The principles involved in electron transfer reactions in these models are shown to be very similar to those of native proteins which follow the Michaelis–Menten saturation kinetics. From the enzyme-product complex, the product is released by concerted oxidative addition and reductive elimination reactions on the central atom (Mo) of the enzyme and that of the substrate in the reductive class of enzymes and the reverse sequence happens in the oxidase class of enzymes.

Print publication date: 29 Sep 2016
Copyright year: 2017
Print ISBN: 978-1-78262-877-4
PDF eISBN: 978-1-78262-882-8
ePub eISBN: 978-1-78262-883-5
From the book series: