Saumen Chakraborty, Ph.D.
Affiliations: | 2011 | University of Michigan, Ann Arbor, Ann Arbor, MI |
Area:
Synthetic Inorganic and Bioinorganic ChemistryGoogle:
"Saumen Chakraborty"Mean distance: 8.81 | S | N | B | C | P |
Parents
Sign in to add mentor| Vincent L. Pecoraro | grad student | 2011 | University of Michigan | |
| (Designed metalloproteins: From structurally characterized scaffolds to helical bundles.) | ||||
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Publications
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| Selvan D, Chakraborty S. (2023) A De Novo Designed Trimeric Metalloprotein as a Ni Model of the Acetyl-CoA Synthase. International Journal of Molecular Sciences. 24 |
| Prasad P, Selvan D, Chakraborty S. (2020) Biosynthetic Approaches Towards the Design of Artificial Hydrogen Evolution Catalysts. Chemistry (Weinheim An Der Bergstrasse, Germany) |
| Selvan D, Prasad P, Farquhar ER, et al. (2019) Redesign of a Copper Storage Protein into an Artificial Hydrogenase. Acs Catalysis. 9: 5847-5859 |
| Selvan D, Prasad P, Crane S, et al. (2019) Intrinsically fluorescent gold nanoclusters stabilized within a copper storage protein that follow the Irving-Williams trend in metal ion sensing. The Analyst |
| Chen Y, Phipps ML, Werner JH, et al. (2018) DNA Templated Metal Nanoclusters: From Emergent Properties to Unique Applications. Accounts of Chemical Research |
| Chakraborty S, Pallada S, Pedersen JT, et al. (2017) Nanosecond Dynamics at Protein Metal Sites: An Application of Perturbed Angular Correlation (PAC) of γ-Rays Spectroscopy. Accounts of Chemical Research |
| Reed JH, Shi Y, Zhu Q, et al. (2017) Manganese and Cobalt in the Nonheme Metal-binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-inactive Mechanism. Journal of the American Chemical Society |
| Bhagi-Damodaran A, Michael MA, Zhu Q, et al. (2017) Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases. Nature Chemistry. 9: 257-263 |
| Stachura M, Chakraborty S, Gottberg A, et al. (2016) Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site. Journal of the American Chemical Society |
| Matsumura H, Chakraborty S, Reed J, et al. (2016) Effect of outer-sphere sidechain substitutions on the fate of the trans iron-nitrosyl dimer in heme/nonheme engineered myoglobins (FeBMbs): Insights into the mechanism of denitrifying NO reductases. Biochemistry |