Research

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Synthetic Biology underpins advances in the bioeconomy

Biological systems - including the simplest cells - exhibit a broad range of functions to thrive in their environment. Research in the Imperial College Centre for Synthetic Biology is focused on the possibility of engineering the underlying biochemical processes to solve many of the challenges facing society, from healthcare to sustainable energy. In particular, we model, analyse, design and build biological and biochemical systems in living cells and/or in cell extracts, both exploring and enhancing the engineering potential of biology. 

As part of our research we develop novel methods to accelerate the celebrated Design-Build-Test-Learn synthetic biology cycle. As such research in the Centre for Synthetic Biology highly multi- and interdisciplinary covering computational modelling and machine learning approaches; automated platform development and genetic circuit engineering ; multi-cellular and multi-organismal interactions, including gene drive and genome engineering; metabolic engineering; in vitro/cell-free synthetic biology; engineered phages and directed evolution; and biomimetics, biomaterials and biological engineering.

Publications

Citation

BibTex format

@article{Varghese:2019:10.1074/jbc.RA118.007285,
author = {Varghese, F and Kabasakal, BV and Cotton, CA and Schumacher, J and Rutherford, AW and Fantuzzi, A and Murray, JW},
doi = {10.1074/jbc.RA118.007285},
journal = {Journal of Biological Chemistry},
pages = {9367--9376},
title = {A low-potential terminal oxidase associated with the iron-only nitrogenase from the nitrogen-fixing bacterium Azotobacter vinelandii},
url = {http://dx.doi.org/10.1074/jbc.RA118.007285},
volume = {294},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The biological route for nitrogen gas entering the biosphere is reduction to ammonia by the nitrogenase enzyme, which is inactivated by oxygen. Three types of nitrogenase exist, the least studied of which is the iron-only nitrogenase. The Anf3 protein in the bacterium Rhodobacter capsulatus is essential for diazotrophic (i.e. nitrogen-fixing) growth with the iron-only nitrogenase, but its enzymatic activity and function are unknown. Here, we biochemically and structurally characterize Anf3 from the model diazotrophic bacterium Azotobacter vinelandii. Determining the Anf3 crystal structure to atomic resolution, we observed that it is a dimeric flavocytochrome with an unusually close interaction between the heme and the flavin adenine dinucleotide cofactors. Measuring the reduction potentials by spectroelectrochemical redox titration, we observed values of -420 ± 10 mV and -330 ± 10 mV for the two FAD potentials and -340 ± 1 mV for the heme. We further show that Anf3 accepts electrons from spinach ferredoxin and that Anf3 consumes oxygen without generating superoxide or hydrogen peroxide. We predict that Anf3 protects the iron-only nitrogenase from oxygen inactivation by functioning as an oxidase in respiratory protection, with flavodoxin or ferredoxin as the physiological electron donors.
AU  - Varghese,F
AU  - Kabasakal,BV
AU  - Cotton,CA
AU  - Schumacher,J
AU  - Rutherford,AW
AU  - Fantuzzi,A
AU  - Murray,JW
DO  - 10.1074/jbc.RA118.007285
EP  - 9376
PY  - 2019///
SN  - 0021-9258
SP  - 9367
TI  - A low-potential terminal oxidase associated with the iron-only nitrogenase from the nitrogen-fixing bacterium Azotobacter vinelandii
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.RA118.007285
UR  - https://www.ncbi.nlm.nih.gov/pubmed/31043481
UR  - http://hdl.handle.net/10044/1/70417
VL  - 294
ER  -
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