Colin Douglas

Affiliations: 
2009-2015 Chemistry University of Toronto, Toronto, ON, Canada 
 2015-2017 Biochemistry Dalhousie University, Halifax, Nova Scotia, Canada 
Google:
"Colin Douglas"
Mean distance: (not calculated yet)
 
BETA: Related publications

Publications

You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect.

McGary LC, Fetter CM, Gu M, et al. (2024) Interrogating l-fuconate dehydratase with tartronate and 3-hydroxypyruvate reveals subtle differences within the mandelate racemase-subgroup of the enolase superfamily. Archives of Biochemistry and Biophysics. 109924
Douglas CD, Grandinetti L, Easton NM, et al. (2021) Slow-Onset, Potent Inhibition of Mandelate Racemase by 2-Formylphenylboronic Acid. An Unexpected Adduct Clasps with the Catalytic Machinery. Biochemistry
Fetter CM, Morrison ZA, Nagar M, et al. (2019) Altering the Y137K164K166 triad of mandelate racemase and its effect on the observed pK of the brønsted base catalysts. Archives of Biochemistry and Biophysics
Lacasse MJ, Douglas CD, Zamble DB. (2016) Mechanism of Selective Nickel Transfer from HypB to HypA, Escherichia coli [NiFe]-Hydrogenase Accessory Proteins. Biochemistry. 55: 6821-6831
Sydor AM, Jost M, Ryan KS, et al. (2013) Metal binding properties of Escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases. Biochemistry. 52: 1788-1801
Douglas CD, Ngu TT, Kaluarachchi H, et al. (2013) Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins. Biochemistry. 52: 6030-9
Sydor AM, Jost M, Ryan KS, et al. (2013) Correction to Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases Biochemistry. 52: 4105-4105
Douglas CD, Dias AV, Zamble DB. (2012) The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB. Dalton Transactions (Cambridge, England : 2003). 41: 7876-8
See more...