ArticleNature chemistry2015
Significantly shorter Fe-S bond in cytochrome P450-I is consistent with greater reactivity relative to chloroperoxidase.
Article in Nature chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 109 citations in OpenAlex.
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- Electronic Modification of a Reduced Mononuclear Nonheme Iron Nitrosyl Complex Leads to HNO Release.Journal of the American Chemical Society · 2025Article
- Spectroscopic Interrogation of Thiolate Hydrogen Bonding in the CO Sensor Protein CooA: Implications for Thiolate Ligation Stability and Cytochrome P450 Function.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Exploring the influence of H-bonding and ligand constraints on thiolate ligated non-heme iron mediated dioxygen activation.Chemical science · 2024Article
- Axial Ligation Impedes Proton-Coupled Electron-Transfer Reactivity of a Synthetic Compound-I Analogue.Journal of the American Chemical Society · 2024Article
- Enhanced Reactivities of Iron(IV)-Oxo Porphyrin Species in Oxidation Reactions Promoted by Intramolecular Hydrogen-Bonding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Axially Coordinated Gold Nanoclusters Tailoring Fe-N-C Nanozymes for Enhanced Oxidase-Like Specificity and Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- The role of basicity in selective C-H bond activation by transition metal-oxidos.Dalton transactions (Cambridge, England : 2003) · 2023Review
- Solvent isotope effects in the catalytic cycle of P450 CYP17A1: Computational modeling of the hydroxylation and lyase reactions.Journal of inorganic biochemistry · 2023Article
- Chemodivergent C(spNature catalysis · 2023Article
- Investigating the Active Oxidants Involved in Cytochrome P450 Catalyzed Sulfoxidation Reactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Mechanism of Melatonin Metabolism by CYP1A1: What Determines the Bifurcation Pathways of Hydroxylation versus Deformylation?The journal of physical chemistry. B · 2022Article
- Article
- Electronic Structure and Reactivity of Dioxygen-Derived Aliphatic Thiolate-Ligated Fe-Peroxo and Fe(IV) Oxo Compounds.Journal of the American Chemical Society · 2022Article
- NRVS investigation of ascorbate peroxidase compound II: Observation of Iron(IV)oxo stretching.Journal of inorganic biochemistry · 2021Article
- Increasing reactivity by incorporating π-acceptor ligands into coordinatively unsaturated thiolate-ligated iron(II) complexes.Inorganica chimica acta · 2021Article
- A safety cap protects hydrogenase from oxygen attack.Nature communications · 2021Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome P450 (P450) and chloroperoxidase (CPO) are thiolate-ligated haem proteins that catalyse the activation of carbon hydrogen bonds. The principal intermediate in these reactions is a ferryl radical species called compound I. P450 compound I (P450-I) is significantly more reactive than CPO-I, which only cleaves activated C-H bonds. To provide insight into the differing reactivities of these intermediates, we examined CPO-I and P450-I using variable-temperature Mössbauer and X-ray absorption spectroscopies. These measurements indicate that the Fe-S bond is significantly shorter in P450-I than in CPO-I. This difference in Fe-S bond lengths can be understood in terms of variations in the hydrogen-bonding patterns within the 'cys-pocket' (a portion of the proximal helix that encircles the thiolate ligand). Weaker hydrogen bonding in P450-I results in a shorter Fe-S bond, which enables greater electron donation from the axial thiolate ligand. This observation may in part explain P450's greater propensity for C-H bond activation.
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