[ccp4bb] PhD available

["Murray, James W" <j.w.murray@IMPERIAL.AC.UK>]

Dear all, 

I have a PhD available, deadline 12th March, on the structural biology of nitrogenase oxygen protection. Please email me if you are interested. Normal UKRI funding rules apply.

https://www.imperial.ac.uk/life-sciences/postgraduate/research/phd-opportunities/

best wishes

James

Biological nitrogen fixation is catalysed by nitrogenase. Nitrogenase is a complex enzyme, with three subunits, binding several cofactors. The best studied nitrogenase has molybdenum in the active site, and is encoded by nif genes. The nif operon encodes other assembly factors and conserved proteins of unknown function. Two alternative nitrogenases, with vanadium or iron instead of molybdenum, encoded by vnf and anf clusters, are even less well-characterised. Nitrogenase is inactivated by oxygen, and this vulnerability, combined with the complicated assembly, makes heterologous expression of nitrogenase challenging. However, expression of nitrogenase in crop plants could revolutionise agriculture, by ending the need for polluting nitrogenous fertilizers.

We have recently biochemically and structurally characterised the Anf3 protein (Fig 1), which protects the iron-only nitrogenase from oxygen. Anf3 is associated with two other conserved genes anf12, which are of unknown function but also essential for iron-only nitrogenase. Our work on the oxygen-protective FeSII protein (PDB 5FRT), is a prerequisite to determining the mechanism of nitrogenase protection. In this project we will structurally and functionally characterise the remaining nif and alternative nitrogenase genes. This will require biochemistry and X-ray crystallography in the Murray group, and biophysical techniques such as EPR and spectroelectrochemistry for the bioinorganic chemistry in the Rutherford group.


--
Dr. James W. Murray
Senior Lecturer, Dept. Life Sciences
Imperial College, London



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