N. Khadka

发表

The human mitochondrial enzyme BCO2 exhibits catalytic activity toward carotenoids and apocarotenoids

L. D. Thomas, M. Golczak, P. Kiser, 2020, The Journal of Biological Chemistry.

Insights into the pathogenesis of dominant retinitis pigmentosa associated with a D477G mutation in RPE65

Elliot H. Choi, K. Palczewski, Susie Suh, 2018, Human molecular genetics.

Evidence for distinct rate-limiting steps in the cleavage of alkenes by carotenoid cleavage dioxygenases

P. Kiser, J. von Lintig, E. Farquhar, 2019, The Journal of Biological Chemistry.

Structure of L509V CAO1 - growth condition 2

P. Kiser, E. Farquhar, W. Shi, 2019 .

Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements.

A. Fielding, L. Seefeldt, B. Hoffman, 2016, Israel journal of chemistry.

Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Journal of the American Chemical Society.

Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride (Janus) State Involves a FeMo-cofactor-H2 Intermediate.

L. Seefeldt, B. Hoffman, D. Dean, 2017, Inorganic chemistry.

Reversible Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride State, the E(4)(4H) Janus Intermediate.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Journal of the American Chemical Society.

Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.

L. Seefeldt, B. Hoffman, D. Dean, 2015, Journal of the American Chemical Society.

On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase

L. Seefeldt, B. Hoffman, D. Dean, 2013, Proceedings of the National Academy of Sciences.

Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein

Ross D. Milton, L. Seefeldt, S. Minteer, 2016 .

Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E2(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis

L. Seefeldt, B. Hoffman, D. Dean, 2018, Inorganic chemistry.

Mechanism of substrate reduction by nitrogenase

N. Khadka, 2017 .

The Structural and Biochemical Basis of Apocarotenoid Processing by β-Carotene Oxygenase-2.

L. D. Thomas, M. Golczak, P. Kiser, 2021, ACS chemical biology.

Light-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid

Gordana Dukovic, J. W. Peters, Molly B. Wilker, 2016, Science.

Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center

Jianye Zhang, P. Kiser, R. Stenkamp, 2021, The Journal of biological chemistry.

Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase

Jianye Zhang, P. Kiser, J. von Lintig, 2020, Proceedings of the National Academy of Sciences.

Mechanism of Nitrogenase H2 Formation by Metal-Hydride Protonation Probed by Mediated Electrocatalysis and H/D Isotope Effects.

Ross D. Milton, L. Seefeldt, S. Minteer, 2017, Journal of the American Chemical Society.

Cluster-Dependent Charge-Transfer Dynamics in Iron-Sulfur Proteins.

D. Goodin, M. Adams, L. Seefeldt, 2018, Biochemistry.

CO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Inorganic chemistry.

Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Journal of the American Chemical Society.