Monooxygenase activity of type 3 copper proteins
Article Abstract:
A investigation, both in the model systems and in the enzymatic systems, is done, determine the molecular mechanism of the monooxygenase (phenolase) activity of type 3 copper proteins. It is observed that the coordination of phenolic oxygen to one of the copper ions of the [Cu.sub.2][O.sub.2] core is necessary for inducing the transfer of the oxygen atom from the peroxo complex to substrate via an electrophilic aromatic substitution mechanism, in both the systems.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2007
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Reversible binding of heme to proteins in cellular signal transduction
Article Abstract:
The new role of heme in cellular signal transduction, and its mechanism that involves reversible binding of heme to proteins apart from its role in numerous biological phenomena is presented. The novel function of heme as an intracellular messenger in the regulation of gene expression and ion channel function is highlighted.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
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