Mutations targeting as few as four residues lining the access tunnel extended the half‐life of an enzyme in 40 % dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 19 °C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active‐site accessibility for cosolvent molecules (red dots).

Mutationen von vier Resten entlang des Zugangstunnels verlängerten die Halbwertzeit eines Enzyms in 40 % Dimethylsulfoxid von Minuten zu Wochen und erhöhten die Schmelztemperatur um 19 °C. Proteinkristallographie und Moleküldynamik zeigen, dass die Packung der Tunnelreste entscheidend für die Proteinstabilität und die Zugänglichkeit des aktiven Zentrums für Cosolvens‐Moleküle (rote Punkte) ist.

Present work reveals the study of catalytic properties of copper and cobalt complexes with phthalocyanine ligands with o-carboxyphenoxy/carboxyphenylsulfanyl/carboxyphenylamino -substituents in the peripheral positions of the macroring. For compounds, the aggregative behavior in aqueous and aqueous -alkaline media was studied. On the example of the reaction of catalytic oxidation of sodium N,N -diethyldithiocarbamate, the rate constants of the fo rmation of the corresponding disulfide were determined. The influence of the nature of the spacer fragment of the p eripheral substituent on the activity of the complexes as catalysts for liquid -phase oxidation was revealed.

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