Biocatalysis is the use of biological systems, particularly enzymes, to speed up chemical reactions. 

Enzymes carry out highly specific reactions 

Advantages of other methods


Nitrogen capture

Cofactor F420

Continuous flow

Relevant Recent Publications

One-pot multi-enzymatic transformatino of NH3, CO2 and ornithine into the organic plant fertilizer citrulline using a single recombinant lysate of E. coli. (2019) Alissandratos A, Hartley CJ, French NG, Kim HK, Allen S, Estavillo GM, Scott C & Easton CJ.

Sus Chem Eng.

A revised biosynthetic pathway for the cofactor F420 in prokaryotes (2019) Bashiri G, Antoney JP, Jirgis ENM, Shah MV, Ney B, Copp J, Stutely SM, Sreebhavan S, Palmer B, Middleditch M, Tokuriki N, Greening C, Scott C, Baker EN, & Jackson CJ

Nat. Comms. 10:  1558

PREPRINT: Engineered Enzymes that Retain and Regenerate their Cofactors Enable Continuous-Flow Biocatalysis (2019) Hartley CJ, Williams CC, Scoble JA, Churches QI, North A, French NG, Nebl T, Coia G, Warden AC, SImpson G, Frazen A, Nixon Jensen C, Turner NJ & Scott C


Computer-guided surface engineering for enzyme improvement. (2018) Wilding M, Scott C & Warden AC

Sci. Report 8: 11998

Hyperthermophilic carbamate kinase stability and anabolic in vitro activity at alkaline pH. (2018) Hennessy JE, Latter MJ, Philbrook A, Bartkus D, Kim HK, Oakeshott JG, Scott C, Alissandratos A & Easton CJ. 

Appl. Environ. Microbiol. 84: e02250-17

Reverse engineering: transaminase biocatalyst development using ancestral sequence reconstruction. (2017) Wilding M, Peat TS, Newman J, Scott C & Jermiin LS

Green Chem. 19: 5375-5380


Sugar analog synthesis by in vitro biocatalytic cascade: a comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis. (2017) Hartley CJ, Scoble JM, Williams CC, Quentin QI, Frazer A, French NG, Taylor MC, Coia G, Simpson G, Turner NJ & Scott C

PLoS One 12: e0184183.


An improved and general streamlined phylogenetic protocol applied to the fatty acid desaturase family. (2017) Wilding M, Nachtschatt M, Speight R & Scott C

Mol. Phylogenet. Evol. 115: 50-57


F420H2-dependent reductases promiscuously reduce diverse compounds through a common hydrogenation mechanism(2017) Greening C, Jirapanjawat T, Afroze S, Ney B, Scott C, Pandey G, Lee BM, Russell RJ, Jackson CJ, Oakeshott JG, Taylor MC & Warden AC

Frontiers in Microbiol. 8: 1000 

Cofactor tail length modulates catalysis of bacterial F420-dependent oxidoreductases (2017) Ney B, Carere CR, Sparling R, Jirapanjawat T, Stott MB, Jackson CJ, Oakeshott JG, Warden AC & Greening C

Frontiers in Microbiol 8: 1902

Hacking nature: genetic tools for reprogramming enzymes. (2017) Hartley CJ, Wilding M & Scott C

Microbiol. Austral. 38: 73-53

X-ray crystal structure of a malonate semialdehyde dehydrogenase from Pseudomonas sp. strain AAC(2017) Wilding M, Scott C, Newman J & Peat TS

Acta Cryst F 73: 24-28.


Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC. (2017)  Wilding M, Scott C, Newman J & Peat TS

Acta Cryst F 73: 29-35


F420 and F0 dependent redox reactions: physiology, biochemistry, and applications. (2016) Greening C, Ahmed FH, Mohamed AE, Lee BM, Pandey G, Warden AC, Scott C, Oakeshott JG, Taylor MC & Jackson CJ

Microbiol. Mol. Biol. Review. 80: 451-493


A β-alanine catabolic pathway containing a highly promiscuous ω-transaminase from the 12-aminododecanate-degrading Pseudomonas sp. Strain AAC. (2016) Wilding M, Peat TS, Newman J & Scott C

Appl. Environ. Microbiol.82: 3846-3856.

Identification of novel transaminases from Pseudomonas sp. strain ACC. (2016) Wilding M, Walsh E, Dorrian S & Scott C

Microbial Biotechnol 8: 665-672.

​​Determination of the structure of the catabolic N-succinylornithine transaminase (AstC) from Escherichia coli(2013) Newman J, Seabrook S, Surjadi R, Williams CC, Lucent D, Wilding M, Scott C & Peat TS

PLoS One 8: e58298


F420-Dependent Enzymes – Potential for Applications in Biotechnology.(2012) Taylor MC, Scott C & Grogan G

Trends Biotechnol. 31: 63-64​

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