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Published on: July 9, 2015
Role of Propionate Side Chain in Heme-Containing Metalloenzymes
Dinesh Singh1, Vandana Kardam1, Kshatresh Dutta Dubey1
1Molecular Simulation Lab, Department of Chemistry, School of Natural Sciences, Shiv Nadar Institution of Eminence Delhi NCR, Gautam Buddha Nagar 201314, India.
None:
Propionate side chains are essential structural components of porphyrin-based metalloenzymes. While numerous studies have investigated the functional significance of propionate side chains from various perspectives, comprehensive reviews focusing specifically on their roles in catalytic mechanisms remain scarce. Traditionally, the role of propionate has been limited to substrate binding and heme stabilization; however, emerging evidence from studies published particularly after 2005 highlights its involvement in a range of noncanonical functions, including water gating, oxidant formation, and electron transfer. This review aims to bridge the gap in existing literature by systematically discussing these expanded roles and emphasizing the broader mechanistic importance of propionate side chains in metalloenzymes, particularly the iron-containing enzymes.
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