A synthetic enzyme is reported that electrocatalytically reduces protons to hydrogen (H₂) in water near neutral pH under aerobic conditions. Cobalt mimochrome VI*a (CoMC6*a) is a mini-protein with a cobalt deuteroporphyrin active site within a scaffold of two synthetic peptides covalently bound to the porphyrin. Comparison of the activity of CoMC6*a to that of cobalt microperoxidase-11 (CoMP11-Ac), a cobalt porphyrin catalyst with a single “proximal” peptide and no organized secondary structure, reveals that CoMC6*a has significantly enhanced longevity, yielding a turnover number exceeding 230 000, in comparison to 25 000 for CoMP11-Ac. Furthermore, comparison of cyclic voltammograms of CoMC6*a and CoMP11-Ac indicates that the trifluoroethanol-induced folding of CoMC6*a lowers the overpotential for catalytic H₂ evolution by up to 100 mV. These results demonstrate that even a minimal polypeptide matrix can enhance longevity and efficiency of a H₂-evolution catalyst.

Here, we highlight recent findings on the urokinase plasminogen activator (uPA)/uPA receptor (uPAR) system that suggest its potential role as a main orchestrator of fatal progression to pulmonary, kidney, and heart failure in patients with coronavirus. Patients with prolonged background inflammation can present with aberrant inflammatory reactions, well recognized as the main factors that can result in death and probably sustained by a dysregulated uPA/uPAR system. SuPAR, the soluble form of uPAR, represents a biomarker of disease progression, and its levels correlate well with comorbidities associated with the death of patients with coronavirus. New drugs that regulate the uPA/uPAR system could help treat the severe complications of highly pathogenic human coronaviruses (hCoVs), including pandemic coronavirus 2019 (COVID-19).

The rational refinement of function into the heme-protein model Mimochrome VI (MC6) resulted in a new analogue, Fe^III-E²L(TD)-MC6, with an improved peroxidase activity.