Dr Jim Reid
Department of Chemistry
Lecturer in Chemical Biology
+44 114 222 9558
Full contact details
Department of Chemistry
13 Brook Hill
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 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. 220.127.116.11) 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. 18.104.22.168) 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?
- An in vitro Coupled Assay for PEPC with Control of Bicarbonate Concentration. Bio-protocol, 11(24).
- The active site of magnesium chelatase. Nature Plants. View this article in WRRO
- Kinetic modifications of C4 PEPC are qualitatively convergent, but larger in Panicum than in Flaveria. Frontiers in Plant Science, 11. View this article in WRRO
- Lateral gene transfer acts as an evolutionary shortcut to efficient C4 biochemistry. Molecular Biology and Evolution. View this article in WRRO
- The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase. Biochemical Journal. View this article in WRRO
- The coproporphyrin ferrochelatase of Staphylococcus aureus: mechanistic insights into a regulatory iron-binding site. The Biochemical journal, 474(20), 3513-3522. View this article in WRRO
- The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.. FEBS Letters, 590(12), 1687-1693. View this article in WRRO
- Five Glutamic Acid Residues in the C-Terminal Domain of the ChlD Subunit Play a Major Role in Conferring Mg2+Cooperativity upon Magnesium Chelatase. Biochemistry, 54(44), 6659-6662. View this article in WRRO
- Characterization of the magnesium chelatase from Thermosynechococcus elongatus.. Biochem J, 457(1), 163-170.
- The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.. J Biol Chem, 288(40), 28727-28732. View this article in WRRO
- Nonequilibrium isotope exchange reveals a catalytically significant enzyme-phosphate complex in the ATP hydrolysis pathway of the AAA(+) ATPase magnesium chelatase.. Biochemistry, 51(10), 2029-2031.
- Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.. J Biol Chem, 284(49), 33795-33799.
- Direct measurement of metal-ion chelation in the active site of the AAA+ ATPase magnesium chelatase.. Biochemistry, 46(44), 12788-12794.
- Direct measurement of metal ion chelation in the active site of human ferrochelatase.. Biochemistry, 46(27), 8121-8127.
- Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis.. Biochemistry, 44(21), 7603-7612.
- Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.. J Biol Chem, 279(26), 26893-26899.
- Isomerization of the uncomplexed actinidin molecule: Kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation. Biochemical Journal, 378(2), 699-703.
- The ATPase activity of the ChlI subunit of magnesium chelatase and formation of a heptameric AAA+ ring.. Biochemistry, 42(22), 6912-6920.
- Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803.. Biochem J, 371(Pt 2), 351-360.
- Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: Evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion. Biochemical Journal, 372(3), 735-746.
- Current understanding of the function of magnesium chelatase.. Biochem Soc Trans, 30(4), 643-645.
- The coupling of ATP hydrolysis to metal ion insertion into porphyrins by magnesium chelatase. Biochemical Society Transactions, 30(3), A75-A75.
- The coupling of ATP hydrolysis to metal ion insertion into porphyrins by magnesium chelatase. Biochemical Society Transactions, 30(3), A50-A50.
- Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex.. Biochemistry, 40(31), 9291-9299.
- Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations. Biochemical Journal, 357(2), 343-352.
- Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations. Biochemical Journal, 357(2), 343-343.
- Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation. BIOCHEM J, 352, 435-441.
- NADPH:protochlorophyllide oxidoreductase from Synechocystis: overexpression, purification and preliminary characterisation.. FEBS Lett, 483(1), 47-51.
- Detection of a free enzyme isomerisation in actinidin catalysed hydrolysis. Biochemical Society Transactions, 26(2), S173-S173.
- A Classical Enzyme Active Center Motif Lacks Catalytic Competence until Modulated Electrostatically†. Biochemistry, 36(33), 9968-9982.
- ACTINIDIN AND CHYMOPAPAIN B PROVIDE VARIATION IN THE COMMON ELECTROSTATIC ENVIRONMENT OF GLU50 IN PAPAIN AND CARICAIN. Biochemical Society Transactions, 25(1), 89S-89S.
- Teaching interests
- Teaching activities
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.
- Skills for Success: Enterprise Project.
- Level 3 Literature Review
- Biological Molecules 2 (Level 2)