Dr Jim Reid

Jim Reid

Lecturer in Chemical Biology
Department of Chemistry
The University of Sheffield
Brook Hill
Sheffield S3 7HF
United Kingdom

Telephone: +44 (0) 114 222 9558
Email: j.reid@sheffield.ac.uk

Reid Group Website

Biographical Sketch

Dr. Reid obtained a BSc in Biochemistry from the University of St. Andrews in 1994, which was followed by a PhD from Queen Mary, University of London. In 1998 he became a postdoctoral researcher at the University of Sheffield, which was followed by an appointment as postdoctoral researcher at Albert Einstein College of Medicine, New York. In 2005 he was appointed as lecturer in Chemical Biology at the University of Sheffield.

Professional Qualifications & Memberships


Research Keywords

Catalysis, Enzyme mechanism, kinetics, porphyrin, chlorophyll.

Teaching Interests

Biological Chemistry


My interests centre on enzyme mechanism, in particular enzymes involved in porphyrin biosynthesis. Biologically interesting porphyrins include haem, sirohaem, coenzyme F430, and chlorophyll and contain a central metal ion. The metal ion insertion steps in porphyrin biosynthesis are catalysed by a family of specific enzymes – the chelatases. We currently focus on two of these enzymes in particular; magnesium chelatase which inserts a magnesium ion into protoporphyrin IX bound for chlorophyll and ferrochelatase which catalyses the final step in haem biosynthesis. Although they share a porphyrin substrate these two enzymes are very different.

Ferrochelatases (E.C. are small proteins, either monomeric or homodimeric depending on species, that catalyse the energetically favourable insertion of ferrous iron into protoporphyrin IX. Mechanistically these are the best characterised of the metal ion chelatases with spectroscopic and crystallographic evidence suggesting that a deformed non-planar porphyrin is a critical intermediate in the reaction.

On the other hand, Magnesium chelatase (E.C. is a large multimeric enzyme comprising three different types of subunit. The increase in complexity is explained by the Mg2+ insertion being energetically unfavourable; the process requires ATP hydrolysis and distinct protein subunits bind porphyrin and hydrolyse MgATP2-. As the two active sites are on separate subunits the question is, how do the ATPase site and the chelatase site communicate?


Undergraduate and postgraduate taught modules

  • Biological Molecules 2 (Level 2)
    This course introduces the structures and chemical properties of key biological molecules: proteins and nucleic acids.
  • Enzyme Catalysis (Level 4)
    This module describes the chemical basis of enzyme catalysis and the techniques used in establishing how enzymes function at the molecular level.

Support Teaching:

  • Skills for Success: Enterprise Project.
  • Level 3 Literature Review

Laboratory Teaching:


Journal articles