Abstract : This report describes progress towards creating peptide-based artificial hydrogenases for interfacing with electrocatalytic applications. The goal of such catalysts is to create hydrogen production or oxidation systems. Basic research in two areas has been pursued. First, artificial amino acids have been developed to tether diiron carbonyl complexes to designed peptides. Dithiol and phosphine artificial amino acids have been generated by covalent modification of a lysine residue. Additionally, an FMOC-protected phosphine-serine derivative has been prepared that can be used in solid phase peptide synthesis. These methods have been used to incorporate metallocenters into water-exposed locations on alpha-helical and beta-sheet peptides, but the catalytic properties were not modified from the small molecule analogues. In a second avenue of research, two new methods for immobilization of protein electrocatalysts at transparent surfaces have been developed. Proteins can be adsorbed to thin (10 nm) gold modified with an alkyl thiol layer, and the resulting submonolayer protein assembly investigated via both UV-vis spectroscopy and electrochemistry. Functional covalent modification of a silane layer on indium tin oxide could also be used as a biocompatible surface for adsorption of proteins.