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A cobalt-tripeptide complex (CoGGH) is developed as an electrocatalyst for the selective six-electron, eight-proton reduction of nitrite to ammonium in aqueous buffer near neutral pH. The onset potential for nitrite reduction occurs at -0.65 V vs Ag/AgCl (1 M KCl). Controlled potential electrolysis at -0.90 V generates ammonium with a faradaic efficiency of 90 ± 3% and a turnover number of 3550 ± 420 over 5.5 h. CoGGH also catalyzes the reduction of the proposed intermediates nitric oxide and hydroxylamine to ammonium. These results reveal that a simple metallopeptide is an active functional mimic of the complex enzymes cytochrome c nitrite reductase and siroheme-containing nitrite reductase.

There has been great interest in the development of stable, inexpensive, efficient catalysts capable of reducing aqueous protons to hydrogen (H2), an alternative to fossil fuels. While synthetic H2 evolution catalysts have been in development for decades, recently there has been great progress in engineering biomolecular catalysts and assemblies of synthetic catalysts and biomolecules. In this Forum Article, progress in engineering proteins to catalyze H2 evolution from water is discussed. The artificial enzymes described include assemblies of synthetic catalysts and photosynthetic proteins, proteins with cofactors replaced with synthetic catalysts, and derivatives of electron-transfer proteins. In addition, a new catalyst consisting of a thermophilic cobalt-substituted cytochrome c is reported. As an electrocatalyst, the cobalt cytochrome shows nearly quantitative Faradaic efficiency and excellent longevity with a turnover number of >270000.

The cobalt complex of an amino-terminal copper and nickel (ATCUN) motif model tripeptide (CoGGH) is shown to act as an electrocatalyst for hydrogen evolution from water near neutral pH with high Faradaic efficiency. The catalyst performance is not significantly impacted by exposure to oxygen. CoGGH represents a new class of hydrogen evolution catalyst that is straightforward to prepare and to modify.

Biological thiols are essential for maintaining the appropriate redox status of proteins, cells, and organisms.[1] Cysteine (Cys) is an essential amino acid that is involved in protein synthesis, detoxification, and metabolism. Elevated levels of Cys have been associated with neurotoxicity,[2] and Cys deficiency is involved in slowed growth rate, hair depigmentation, edema, lethargy, liver damage, muscle and fat loss, skin lesions, and weakness.[3] Homocysteine (Hcy) has been implicated in various types of vascular and renal diseases. Elevated Hcy in the blood (>12 µm) is a well-known risk factor for cardiovascular[4a] and Alzheimer’s disease,[4b] neutral tube defects, complications during pregnancy, inflammatory bowel disease, and osteoporosis.[4c] Because Cys and Hcy levels are associated with different diseases despite their similar structures, their discrimination is necessary.