Dr. Jim Reid

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.

Research Keywords

Catalysis, Enzyme mechanism, kinetics, porphyrin, chlorophyll.

Teaching Keywords

Biological Chemistry

Selected Publications:

Nonequilibrium Isotope Exchange Reveals a Catalytically Significant Enzyme-Phosphate Complex in the ATP Hydrolysis Pathway of the AAA+ ATPase Magnesium Chelatase, Nathan B.P. Adams and James D. Reid, Biochemistry, 2012, in press.
Metal Ion Selectivity and Substrate Inhibition in the Metal Ion Chelation Catalyzed by Human Ferrochelatase, R. E. Davidson, C. J. Chesters and J. D. Reid, J. Biol. Chem. 2009, 284, 33795-33799.
Direct measurement of metal ion chelation in the active site of human ferrochelatase, M. Hoggins, H. A. Dailey, C. N. Hunter and J. D. Reid, Biochemistry 2007, 46, 8121-8127.
Direct measurement of metal-ion chelation in the active site of the AAA ATPase magnesium chelatase, J. Viney, P. A. Davison, N. C. Hunter and J. D. Reid, Biochemistry 2007, 46, 12788-12794.

Research Interests

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. 4.99.1.1) 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. 6.6.1.1) 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?

Teaching Section

Organic Chemistry

Undergraduate Courses Taught

An Introduction to Biology for Physical Scientists (Year 1)
This unit provides a basic knowledge and understanding of the occurrence, structure and function of important types of biopolymers such as proteins and nucleic acids, their organisation into biomaterials and their function in living systems.
Biological Molecules 2 (Year 2)
This segment introduces the structures and chemical properties of key biological molecules: proteins and nucleic acids.
Enzyme Catalysis (Year 4)
This segment describes the chemical basis of enzyme catalysis and the techniques used in establishing how enzymes function at the molecular level.

Postgraduate Courses Taught

CHM6108: "Biopolymers and Biomaterials"

Tutorial & Workshop Support

First Year General Tutorials.
First Year Workshops.
Second Year Workshops.
Third Year Literature Review.
Fourth Year Workshops.

Laboratory Teaching

Second Year Laboratory Demonstrating
Third Year Advanced Physical Chemistry
Fourth Year Research Project.