Dr Jim Reid
Lecturer in Chemical Biology
Telephone: +44 (0) 114 222 9558
|Reid Group Website|
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
Catalysis, Enzyme mechanism, kinetics, porphyrin, chlorophyll.
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. 184.108.40.206) 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. 220.127.116.11) 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
- Hobbs C, Reid JD & Shepherd M (2017) The coproporphyrin ferrochelatase of Staphylococcus aureus : mechanistic insights into a regulatory iron binding site.. Biochemical Journal. View this article in WRRO
- Adams NB, Brindley AA, Neil Hunter C & Reid JD (2016) The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.. FEBS Lett, 590(12), 1687-1693. View this article in WRRO
- Brindley AA, Adams NBP, Hunter CN & Reid JD (2015) Five glutamic acid residues in the C-terminal domain of the ChlD subunit play a major role in conferring Mg(2+) cooperativity upon magnesium chelatase.. Biochemistry, 54(44), 6659-6662. View this article in WRRO
- Adams NBP, Marklew CJ, Brindley AA, Hunter CN & Reid JD (2014) Characterization of the magnesium chelatase from Thermosynechococcus elongatus.. Biochem J, 457(1), 163-170.
- Adams NBP & Reid JD (2013) 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
- Adams NBP & Reid JD (2012) 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.
- Davidson RE, Chesters CJ & Reid JD (2009) Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.. J Biol Chem, 284(49), 33795-33799.
- Viney J, Davison PA, Hunter CN & Reid JD (2007) Direct measurement of metal-ion chelation in the active site of the AAA+ ATPase magnesium chelatase.. Biochemistry, 46(44), 12788-12794.
- Hoggins M, Dailey HA, Hunter CN & Reid JD (2007) Direct measurement of metal ion chelation in the active site of human ferrochelatase.. Biochemistry, 46(27), 8121-8127.
- Davison PA, Schubert HL, Reid JD, Iorg CD, Heroux A, Hill CP & Hunter CN (2005) Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis.. Biochemistry, 44(21), 7603-7612.
- Reid JD & Hunter CN (2004) Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.. J Biol Chem, 279(26), 26893-26899.
- Reid JD, Hussain S, Bailey TSF, Sonkaria S, Sreedharan SK, Thomas EW, Resmini M & Brocklehurst K (2004) Isomerization of the uncomplexed actinidin molecule: Kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation. Biochemical Journal, 378(2), 699-703.
- Reid JD, Siebert CA, Bullough PA & Hunter CN (2003) The ATPase activity of the ChlI subunit of magnesium chelatase and formation of a heptameric AAA+ ring.. Biochemistry, 42(22), 6912-6920.
- Shepherd M, Reid JD & Hunter CN (2003) Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803.. Biochem J, 371(Pt 2), 351-360.
- Hussain S, Pinitglang S, Bailey TSF, Reid JD, Noble MA, Resmini M, Thomas EW, Greaves RB, Verma CS & Brocklehurst K (2003) 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.
- Reid JD & Hunter CN (2002) Current understanding of the function of magnesium chelatase.. Biochem Soc Trans, 30(4), 643-645.
- Reid JD & Hunter CN (2002) The coupling of ATP hydrolysis to metal ion insertion into porphyrins by magnesium chelatase. Biochemical Society Transactions, 30(3), a75-a75.
- Reid JD & Hunter CN (2002) The coupling of ATP hydrolysis to metal ion insertion into porphyrins by magnesium chelatase. Biochemical Society Transactions, 30(3), a50-a50.
- Karger GA, Reid JD & Hunter CN (2001) Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex.. Biochemistry, 40(31), 9291-9299.
- Reid JD, Hussain S, Sreedharan SK, Bailey TS, Pinitglang S, Thomas EW, Verma CS & Brocklehurst K (2001) Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations.. Biochemical Journal, 357(Pt 2), 343-352.
- Jensen PE, Reid JD & Hunter CN (2000) Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation. BIOCHEM J, 352, 435-441.
- Heyes DJ, Martin GE, Reid RJ, Hunter CN & Wilks HM (2000) NADPH:protochlorophyllide oxidoreductase from Synechocystis: overexpression, purification and preliminary characterisation.. FEBS Lett, 483(1), 47-51.
- REID JAMESD, SREEDHARAN SUNEAL, COLE AMBROSE, MASKELL SCOTT, BOKTH ANJUMON, THOMAS EMRYSW & BROCKLEHURST KEITH (1998) Detection of a free enzyme isomerisation in actinidin catalysed hydrolysis. Biochemical Society Transactions, 26(2), s173-s173.
- Pinitglang S, Watts AB, Patel M, Reid JD, Noble MA, Gul S, Bokth A, Naeem A, Patel H, Thomas EW , Sreedharan SK et al (1997) A classical enzyme active center motif lacks catalytic competence until modulated electrostatically.. Biochemistry, 36(33), 9968-9982.
- REID JAMESD, PINITGLANG SURAPONG, TOPHAM CHRISTOPHERM, VERMA CHANDRA, THOMAS EMRYSW & BROCKLEHURST KEITH (1997) ACTINIDIN AND CHYMOPAPAIN B PROVIDE VARIATION IN THE COMMON ELECTROSTATIC ENVIRONMENT OF GLU50 IN PAPAIN AND CARICAIN. Biochemical Society Transactions, 25(1), 89s-89s.