A Trigonal-Bipyramidal Ferric Aqua Complex with a Sterically Hindered Salen Ligand as a Model for the Active Site of Protocatechuate 3,4-Dioxygenase

✍ Scribed by Hiroshi Fujii; Yasuhiro Funahashi

• Publisher: John Wiley and Sons
• Year: 2002
• Tongue: English
• Weight: 109 KB
• Volume: 41
• Category: Article
• ISSN: 0044-8249
• DOI: 10.1002/1521-3773(20021004)41:19<3638::aid-anie3638>3.0.co;2-#

✦ Synopsis

Protocatechurate 3,4-dioxygenase (3,4-PCD) has been found in soil bacteria and is known to play a role in degrading aromatic molecules in nature. [1, 2] The enzyme is classified as an intradiol dioxygenase and cleaves catechol analogues bound to the iron(iii) site into aliphatic products with incorporation of both atoms of molecular oxygen. It has been proposed that the enzyme does not activate an iron-bound oxygen molecule, but rather induces an iron-bound catecholate to react with O 2 . [2] Therefore, knowledge of the structure and electronic state of the iron site is essential to under-