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Peng, Y. Heme-Thiolate Enzyme. Encyclopedia. Available online: https://encyclopedia.pub/entry/61061 (accessed on 02 November 2026).
Peng Y. Heme-Thiolate Enzyme. Encyclopedia. Available at: https://encyclopedia.pub/entry/61061. Accessed November 02, 2026.
Peng, Yu. "Heme-Thiolate Enzyme" Encyclopedia, https://encyclopedia.pub/entry/61061 (accessed November 02, 2026).
Peng, Y. (2026, October 17). Heme-Thiolate Enzyme. In Encyclopedia. https://encyclopedia.pub/entry/61061
Peng, Yu. "Heme-Thiolate Enzyme." Encyclopedia. Web. 17 October, 2026.

Heme-Thiolate Enzyme

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A heme-thiolate enzyme is an enzyme whose heme iron has an axial sulfur ligand supplied by a cysteine thiolate in the protein. This coordination arrangement contributes to the oxygen-activation chemistry of cytochrome P450 enzymes [1]. A high-valent iron–oxo species, compound I, can cleave substrate carbon–hydrogen bonds during the catalytic cycle [2]. Thiolate donation alters the electronic properties of iron-bound oxygen intermediates and helps support the highly reactive species used in substrate oxidation [3]. In many members, successive reduction and protonation steps lead to oxygen–oxygen bond cleavage and formation of a high-valent iron–oxo intermediate. Reaction with the bound substrate then transfers oxygen or removes hydrogen equivalents, with the surrounding protein controlling substrate orientation and access [4].

cysteine ligation heme iron peroxygenases iron–oxo intermediates
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References

  1. Ilia G. Denisov; Thomas M. Makris; Stephen G. Sligar; Ilme Schlichting; Structure and Chemistry of Cytochrome P450. Chem. Rev. 2005, 105, 2253-2278. [CrossRef]
  2. Jonathan Rittle; Michael T. Green; Cytochrome P450 Compound I: Capture, Characterization, and C-H Bond Activation Kinetics. Science 2010, 330, 933-937. [CrossRef]
  3. François Ogliaro; Nathan Harris; Shimrit Cohen; Michael Filatov; Samuël P. de Visser; Sason Shaik; A Model “Rebound” Mechanism of Hydroxylation by Cytochrome P450: Stepwise and Effectively Concerted Pathways, and Their Reactivity Patterns. J. Am. Chem. Soc. 2000, 122, 8977-8989. [CrossRef]
  4. Bernard Meunier; Samuël P. de Visser; Sason Shaik; Mechanism of Oxidation Reactions Catalyzed by Cytochrome P450 Enzymes. Chem. Rev. 2004, 104, 3947-3980. [CrossRef]
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Update Date: 24 Oct 2026
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