Reid, Jim - University of Sheffield - Department of Chemistry

个人简介

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.

研究领域

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?

近期论文

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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 NB, Marklew CJ, Brindley AA, Hunter CN & Reid JD (2014) Characterization of the magnesium chelatase from Thermosynechococcus elongatus.. Biochem J, 457(1), 163-170. Adams NB & 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 NB & 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.