Reid, Jim, Dr

Dr Jim Reid

School of Mathematical and Physical Sciences

Chemistry Level 4 Coordinator

Lecturer in Chemical Biology

j.reid@sheffield.ac.uk
+44 114 222 9558

Dainton Building

Full contact details

Dr Jim Reid
School of Mathematical and Physical Sciences
Dainton Building
13 Brook Hill
��«Ӱҵ
S3 7HF

Profile: 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 ��«Ӱҵ, 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 ��«Ӱҵ.

Qualifications: FHEA

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?

Publications

Journal articles

Moody NR, Phansopal C & Reid JD (2021) . Bio-protocol, 11(24).
Adams NBP, Bisson C, Brindley AA, Farmer DA, Davison PA, Reid JD & Hunter CN (2020) . Nature Plants.
Moody NR, Christin P-A & Reid JD (2020) . Frontiers in Plant Science, 11.
Phansopa C, Dunning LT, Reid JD & Christin P-A (2020) . Molecular Biology and Evolution.
Farmer DA, Brindley AA, Hitchcock A, Jackson PJ, Johnson B, Dickman MJ, Hunter CN, Reid JD & Adams NBP (2019) . Biochemical Journal.
Hobbs C, Reid JD & Shepherd M (2017) . The Biochemical journal, 474(20), 3513-3522.
Adams NB, Brindley AA, Neil Hunter C & Reid JD (2016) . FEBS Letters, 590(12), 1687-1693.
Brindley AA, Adams NBP, Hunter CN & Reid JD (2015) . Biochemistry, 54(44), 6659-6662.
Adams NBP, Marklew CJ, Brindley AA, Hunter CN & Reid JD (2014) . Biochem J, 457(1), 163-170.
Adams NBP & Reid JD (2013) . J Biol Chem, 288(40), 28727-28732.
Adams NBP & Reid JD (2012) . Biochemistry, 51(10), 2029-2031.
Davidson RE, Chesters CJ & Reid JD (2009) . J Biol Chem, 284(49), 33795-33799.
Viney J, Davison PA, Hunter CN & Reid JD (2007) . Biochemistry, 46(44), 12788-12794.
Hoggins M, Dailey HA, Hunter CN & Reid JD (2007) . Biochemistry, 46(27), 8121-8127.
Davison PA, Schubert HL, Reid JD, Iorg CD, Heroux A, Hill CP & Hunter CN (2005) . Biochemistry, 44(21), 7603-7612.
Reid JD & Hunter CN (2004) . J Biol Chem, 279(26), 26893-26899.
Reid JD, Hussain S, Bailey TSF, Sonkaria S, Sreedharan SK, Thomas EW, Resmini M & Brocklehurst K (2004) . Biochemical Journal, 378(2), 699-703.
Reid JD, Siebert CA, Bullough PA & Hunter CN (2003) . Biochemistry, 42(22), 6912-6920.
Shepherd M, Reid JD & Hunter CN (2003) . 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) . Biochemical Journal, 372(3), 735-746.
Reid JD & Hunter CN (2002) . Biochem Soc Trans, 30(4), 643-645.
Reid JD & Hunter CN (2002) . Biochemical Society Transactions, 30(3), A75-A75.
Reid JD & Hunter CN (2002) . Biochemical Society Transactions, 30(3), A50-A50.
Karger GA, Reid JD & Hunter CN (2001) . Biochemistry, 40(31), 9291-9299.
REID JD, HUSSAIN S, SREEDHARAN SK, BAILEY TSF, PINITGLANG S, THOMAS EW, VERMA CS & BROCKLEHURST K (2001) . Biochemical Journal, 357(2), 343-352.
REID JD, HUSSAIN S, SREEDHARAN SK, BAILEY TSF, PINITGLANG S, THOMAS EW, VERMA CS & BROCKLEHURST K (2001) . Biochemical Journal, 357(2), 343-343.
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) . FEBS Lett, 483(1), 47-51.
REID JD, SREEDHARAN S, COLE A, MASKELL S, BOKTH A, THOMAS EW & BROCKLEHURST K (1998) . 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) . Biochemistry, 36(33), 9968-9982.
REID JD, PINITGLANG S, TOPHAM CM, VERMA C, THOMAS EW & BROCKLEHURST K (1997) . Biochemical Society Transactions, 25(1), 89S-89S.

Teaching interests: Biological Chemistry

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.

Support Teaching:

Skills for Success: Enterprise Project.
Level 3 Literature Review