ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025
Spectroscopic Interrogation of Thiolate Hydrogen Bonding in the CO Sensor Protein CooA: Implications for Thiolate Ligation Stability and Cytochrome P450 Function.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
- EPR spectroscopy reveals glycerol-dependent activation of cysteamine dioxygenase (ADO) enables bidentate substrate coordination.The Journal of biological chemistry · 2026Article
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Authors and funding
5 authors.
Funding
Abstract
Cysteine (Cys) thiolate coordination in hemoproteins is a unique ligation motif found in enzymes and small molecule sensors. It is posited that divergence between these two functional classes of heme thiolate proteins is a result of distinct hydrogen bonding (H-bonding) interactions with the axial Cys(thiolate) ligand. To further test this hypothesis, we report a spectroscopic analysis of thiolate H-bonding in CooA, a carbon monoxide-sensing heme protein from Rhodospirillum rubrum that is known to switch between Cys
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