Electroenzymatic Nitrogen Fixation Using a MoFe Protein System Immobilized in an Organic Redox Polymer.

Authors :: Lee YS
Ruff A
Cai R
Lim K
Schuhmann W
Minteer SD
Source :: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2020 Sep 14; Vol. 59 (38), pp. 16511-16516. Date of Electronic Publication: 2020 Jul 22.
Publication Year :: 2020
Abstract: We report an organic redox-polymer-based electroenzymatic nitrogen fixation system using a metal-free redox polymer, namely neutral-red-modified poly(glycidyl methacrylate-co-methylmethacrylate-co-poly(ethyleneglycol)methacrylate) with a low redox potential of -0.58 V vs. SCE. The stable and efficient electric wiring of nitrogenase within the redox polymer matrix enables mediated bioelectrocatalysis of N <subscript>3</subscript> <superscript>-</superscript> , NO <subscript>2</subscript> <superscript>-</superscript> and N <subscript>2</subscript> to NH <subscript>3</subscript> catalyzed by the MoFe protein via the polymer-bound redox moieties distributed in the polymer matrix in the absence of the Fe protein. Bulk bioelectrosynthetic experiments produced 209±30 nmol NH <subscript>3</subscript> nmol MoFe <superscript>-1</superscript> h <superscript>-1</superscript> from N <subscript>2</subscript> reduction. <superscript>15</superscript> N <subscript>2</subscript> labeling experiments and NMR analysis were performed to confirm biosynthetic N <subscript>2</subscript> reduction to NH <subscript>3</subscript> .<br /> (© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.)

Subjects :: Crystallography, X-Ray
Enzymes, Immobilized chemistry
Enzymes, Immobilized metabolism
Models, Molecular
Molybdoferredoxin chemistry
Nitrogen Fixation
Nitrogenase chemistry
Oxidation-Reduction
Polymers chemistry
Azotobacter vinelandii enzymology
Molybdoferredoxin metabolism
Nitrogenase metabolism
Polymers metabolism

Full Text Access

Tools