Aqueous olefin metathesis: recent developments and applications

• Valerio Sabatino and
• Thomas R. Ward

Beilstein J. Org. Chem. 2019, 15, 445–468, doi:10.3762/bjoc.15.39

• metathase based on the dative anchoring of a biotinylated HG-type catalyst to human carbonic anhydrase II (hCAII) in 2015 [67]. The active site of hCAII contains Zn2+ which is coordinated to three histidines. Catalyst 61 contains an arylsulfonamide moiety that coordinates the metal with high affinity (Kd

Azobenzene-based inhibitors of human carbonic anhydrase II

• Leander Simon Runtsch,
• David Michael Barber,
• Peter Mayer,
• Michael Groll,
• Dirk Trauner and
• Johannes Broichhagen

Beilstein J. Org. Chem. 2015, 11, 1129–1135, doi:10.3762/bjoc.11.127

• interested in the exploration of azobenzene-containing sulfonamides to block the catalytic activity of human carbonic anhydrase II (hCAII). Herein, we report the synthesis and in vitro evaluation of a small library of nine photochromic sulfonamides towards hCAII. All molecules are azobenzene-4-sulfonamides

• kinetics. Keywords: azobenzene chemistry; enzyme inhibitors; human carbonic anhydrase II; sulfonamide; X-ray crystallography; Introduction Carbonic anhydrase (CA) is an ubiquitously found zinc-containing metalloenzyme with many isoforms, which all catalyze the conversion of carbon dioxide and water to

• colorimetrically (Figure 1a, right) [2]. In humans, isoform II (human carbonic anhydrase II; hCAII) is found in many tissues and is responsible for maintaining the inner eye pressure among other regulatory tasks [1]. Consequently, its failure is associated with glaucoma [1][3]. Treatment of this severe disease