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Brett M. Barney

Researcher at University of Minnesota

Publications -  54
Citations -  2580

Brett M. Barney is an academic researcher from University of Minnesota. The author has contributed to research in topics: Nitrogenase & Azotobacter vinelandii. The author has an hindex of 30, co-authored 51 publications receiving 2227 citations. Previous affiliations of Brett M. Barney include Virginia Tech & Arizona State University.

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Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis.

TL;DR: Evidence is provided to indicate that the smaller alkyne substrate acetylene (HC≡CH), the physiological substrate dinitrogen, and its semi-reduced form hydrazine (H2N-NH2) interact with the same Fe-S face of the FeMo-cofactor.
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Breaking the N2 triple bond : insights into the nitrogenase mechanism

TL;DR: A comparison of the current state of knowledge of the trapped species arising from non-physiological substrates and nitrogenous substrates is beginning to reveal some of the intricacies of how nitrogenase breaks the N2 triple bond.
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Characterization of a fatty acyl-CoA reductase from Marinobacter aquaeolei VT8: a bacterial enzyme catalyzing the reduction of fatty acyl-CoA to fatty alcohol.

TL;DR: A novel bacterial enzyme from Marinobacter aquaeolei VT8 is identified, purify, and characterize that catalyzes the reduction of fatty acyl-CoA by four electrons to the corresponding fatty alcohol, eliminating the need for a separate fatty aldehyde reductase.
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Intermediates Trapped during Nitrogenase Reduction of N⋮N, CH3−NNH, and H2N−NH2

TL;DR: In this paper, a high population intermediate has been trapped on the nitrogenase active site FeMo cofactor during reduction of N2 and intermediates have been trapped during CH3−NNH by the α-195Gln variant.