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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