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Biochemistry|September 12, 2008
Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate bindingSarah J Thackray, Chiara Bruckmann, J L Ross Anderson, et al.
Journal of the American Chemical Society|April 1, 2010
Probing the ternary complexes of indoleamine and tryptophan 2,3-dioxygenases by cryoreduction EPR and ENDOR spectroscopyRoman M Davydov, Nishma Chauhan, Sarah J Thackray, et al.
Biochemistry|October 11, 2007
The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamilyWalter De Laurentis, Leang Khim, J L Ross Anderson, et al.
ACS Catalysis|September 24, 2021
Rigidifying a De Novo Enzyme Increases Activity and Induces a Negative Activation Heat CapacitySarah A Hindson, H Adrian Bunzel, Bettina Frank, et al.
Protein Science : a Publication of the Protein Society|July 9, 2024
Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein designBenjamin J Hardy, Paulina Dubiel, Ethan L Bungay, et al.
Journal of the American Chemical Society|November 30, 2020
Controlling Protein Nanocage Assembly with Hydrostatic PressureKristian Le Vay, Ben M Carter, Daniel W Watkins, et al.
Chemical Science|March 18, 2014
Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquetteJ L Ross Anderson, Craig T Armstrong, Goutham Kodali, et al.
ACS Catalysis|June 19, 2020
Rewiring the "Push-Pull" Catalytic Machinery of a Heme Enzyme Using an Expanded Genetic CodeMary Ortmayer, Karl Fisher, Jaswir Basran, et al.
Scientific Reports|October 3, 2018
The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexityChristophe J Lalaurie, Virginie Dufour, Anna Meletiou, et al.
Nature Communications|June 18, 2015
Artificial membrane-binding proteins stimulate oxygenation of stem cells during engineering of large cartilage tissueJames P K Armstrong, Rameen Shakur, Joseph P Horne, et al.
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