Mechanism of the Early Catalytic Events in the Collagenolysis by Matrix Metalloproteinase‐1

Abstract

The front cover artwork is provided by Dr. Karabencheva‐Christova's group at Michigan Technological University. The images show the initially formed and the catalytically productive conformations of MMP‐1 complex with the Triple Helical Peptide (THP), the free energy profile connecting them as well as the coordination geometry of the catalytic zinc (II). The background shows the collagen macromolecule. Read the full text of the Research Article at 10.1002/cphc.202200649.

Unusual catalytic strategy by non-heme Fe(ii)/2-oxoglutarate-dependent aspartyl hydroxylase AspH

“…The results align with earlier studies that demonstrated the role of dynamics for substrate binding, catalysis and as a valuable tool for enzyme engineering together with other computational and experimental approaches. 99,136,137,[197][198][199][200][201][202][203] How the substrate Asp103 hFX binding mode A inuence the catalytic reaction of dioxygen activation? The high spin quintet state of Fe(III)-O-Oc − is reported to be the most favorable spin state for dioxygen activation in non-heme dioxygenases.…”