Volume 101, 2005

28  Bioinorganic chemistry

Abstract

During 2004 two exciting X-ray crystal structures of potentially reactive intermediates in the catalytic cycles of two Cu-containing enzymes, peptidylglycine α-hydroxylating monooxygenase and nitrite reductase, have been solved. The solution of the X-ray crystal structure of photosystem II from Thermosynechococcus eleongatus at 3.5 Å resolution has been a major achievement and provides considerable insight into the nature of the manganese-containing oxygen evolving centre. Significant progress has been made in the elucidation of the sequence of biological events that lead to the assembly of the molybdopterin unit and its coordination to Mo as the molybdenum cofactor at the active sites of Mo-containing enzymes.

Article information

Article type
Review Article
First published
09 Jun 2005

Annu. Rep. Prog. Chem., Sect. A: Inorg. Chem., 2005,101, 607-630

28  Bioinorganic chemistry

J. McMaster, Annu. Rep. Prog. Chem., Sect. A: Inorg. Chem., 2005, 101, 607 DOI: 10.1039/B413630F

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