title: Self-assembling biomolecular catalysts for hydrogen production.
abstract: The chemistry of highly evolved protein-based compartments has inspired the design of new catalytically active materials that self-assemble from biological components. A frontier of this biodesign is the potential to contribute new catalytic systems for the production of sustainable fuels, such as hydrogen. Here, we show the encapsulation and protection of an active hydrogen-producing and oxygen-tolerant [NiFe]-hydrogenase, sequestered within the capsid of the bacteriophage P22 through directed self-assembly. We co-opted Escherichia coli for biomolecular synthesis and assembly of this nanomaterial by expressing and maturing the EcHyd-1 hydrogenase prior to expression of the P22 coat protein, which subsequently self assembles. By probing the infrared spectroscopic signatures and catalytic activity of the engineered material, we demonstrate that the capsid provides stability and protection to the hydrogenase cargo. These results illustrate how combining biological function with directed supramolecular self-assembly can be used to create new materials for sustainable catalysis.
authors.affiliation: Department of Chemistry, Indiana University, Bloomington, Indiana 47407-7102, USA.|Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, USA.
authors.forename: Paul C
authors.initials: PC
authors.lastname: Jordan
authors.affiliation: Department of Chemistry &Biochemistry, University of Texas at Tyler, Tyler, Texas 75799, USA.
authors.forename: Dustin P
authors.initials: DP
authors.lastname: Patterson
authors.affiliation: Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, USA.
authors.forename: Kendall N
authors.initials: KN
authors.lastname: Saboda
authors.affiliation: Department of Chemistry, Indiana University, Bloomington, Indiana 47407-7102, USA.|Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, USA.
authors.forename: Ethan J
authors.initials: EJ
authors.lastname: Edwards
authors.affiliation: Department of Microbiology &Immunology, Montana State University, Bozeman, Montana 59717, USA.
authors.forename: Heini M
authors.initials: HM
authors.lastname: Miettinen
authors.affiliation: Department of Biophysics, Bose Institute, Kolkata 700054, India.
authors.forename: Gautam
authors.initials: G
authors.lastname: Basu
authors.affiliation: Department of Chemistry, Indiana University, Bloomington, Indiana 47407-7102, USA.
authors.forename: Megan C
authors.initials: MC
authors.lastname: Thielges
authors.affiliation: Department of Chemistry, Indiana University, Bloomington, Indiana 47407-7102, USA.
authors.forename: Trevor
authors.initials: T
authors.lastname: Douglas
mesh_terms: D002384:Catalysis; D004926:Escherichia coli / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry*
chemical_list: D006859:Hydrogen; C043296:nickel-iron hydrogenase; D006864:Hydrogenase