ReviewACS organic & inorganic Au2025
Role of Propionate Side Chain in Heme-Containing Metalloenzymes.
Review in ACS organic & inorganic Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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3 authors.
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Abstract
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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