Mechanistic Insights into the N‐Hydroxylations Catalyzed by the Binuclear Iron Domain of SznF Enzyme: Key Piece in the Synthesis of Streptozotocin
SznF, a member of the emerging family of heme‐oxygenase‐like (HO‐like) di‐iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion of Nω‐methyl‐L‐arginine (L‐NMA) into N‐nitroso‐containing product, which can subsequently be transformed into streptozotocin. Using unrestri...
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Published in | Chemistry : a European journal Vol. 30; no. 16; pp. e202303845 - n/a |
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Language | English |
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15.03.2024
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Abstract | SznF, a member of the emerging family of heme‐oxygenase‐like (HO‐like) di‐iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion of Nω‐methyl‐L‐arginine (L‐NMA) into N‐nitroso‐containing product, which can subsequently be transformed into streptozotocin. Using unrestricted density functional theory (UDFT) with the hybrid functional B3LYP, we have mechanistically investigated the two sequential hydroxylations of L‐NMA catalyzed by SznF's binuclear iron central domain. Mechanism B primarily involves the O−O bond dissociation, forming Fe(IV)=O, induced by the H+/e− introduction to the FeA side of μ‐1,2‐peroxo‐Fe2(III/III), the substrate hydrogen ion by Fe(IV)=O, and the hydroxyl rebound to the substrate N radical. The stochastic addition of H+/e− to the FeB side (mechanism C) can transition to mechanism B, thereby preventing enzyme deactivation. Two other competing mechanisms, involving the direct O−O bond dissociation (mechanism A) and the addition of H2O as a co‐substrate (mechanism D), have been ruled out.
Enzyme catalysis: The consecutive hydroxylation mechanism of Nω‐methyl‐L‐arginine (L‐NMA) catalyzed by SznF's di‐iron domain is presented. Initiated by the peroxo‐Fe2(III/III) intermediate, the reaction involves proton/electron (H+/e−) addition on either side of this intermediate facilitating the generation of Nδ‐hydroxy‐Nω‐methyl‐L‐arginine (L‐HMA) and Nδ‐hydroxy‐Nω‐hydroxy‐Nω‐methyl‐L‐arginine (L–DHMA). |
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AbstractList | Abstract
SznF, a member of the emerging family of heme‐oxygenase‐like (HO‐like) di‐iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion of N
ω
‐methyl‐L‐arginine (L‐NMA) into N‐nitroso‐containing product, which can subsequently be transformed into streptozotocin. Using unrestricted density functional theory (UDFT) with the hybrid functional B3LYP, we have mechanistically investigated the two sequential hydroxylations of L‐NMA catalyzed by SznF's binuclear iron central domain. Mechanism B primarily involves the O−O bond dissociation, forming Fe(IV)=O, induced by the H
+
/e
−
introduction to the Fe
A
side of μ‐1,2‐peroxo‐Fe
2
(III/III), the substrate hydrogen abstraction by Fe(IV)=O, and the hydroxyl rebound to the substrate N radical. The stochastic addition of H
+
/e
−
to the Fe
B
side (mechanism C) can transition to mechanism B, thereby preventing enzyme deactivation. Two other competing mechanisms, involving the direct O−O bond dissociation (mechanism A) and the addition of H
2
O as a co‐substrate (mechanism D), have been ruled out. SznF, a member of the emerging family of heme‐oxygenase‐like (HO‐like) di‐iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion of Nω‐methyl‐L‐arginine (L‐NMA) into N‐nitroso‐containing product, which can subsequently be transformed into streptozotocin. Using unrestricted density functional theory (UDFT) with the hybrid functional B3LYP, we have mechanistically investigated the two sequential hydroxylations of L‐NMA catalyzed by SznF's binuclear iron central domain. Mechanism B primarily involves the O−O bond dissociation, forming Fe(IV)=O, induced by the H+/e− introduction to the FeA side of μ‐1,2‐peroxo‐Fe2(III/III), the substrate hydrogen abstraction by Fe(IV)=O, and the hydroxyl rebound to the substrate N radical. The stochastic addition of H+/e− to the FeB side (mechanism C) can transition to mechanism B, thereby preventing enzyme deactivation. Two other competing mechanisms, involving the direct O−O bond dissociation (mechanism A) and the addition of H2O as a co‐substrate (mechanism D), have been ruled out. SznF, a member of the emerging family of heme-oxygenase-like (HO-like) di-iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion of Nω-methyl-L-arginine (L-NMA) into N-nitroso-containing product, which can subsequently be transformed into streptozotocin. Using unrestricted density functional theory (UDFT) with the hybrid functional B3LYP, we have mechanistically investigated the two sequential hydroxylations of L-NMA catalyzed by SznF's binuclear iron central domain. Mechanism B primarily involves the O-O bond dissociation, forming Fe(IV)=O, induced by the H+/e- introduction to the FeA side of μ-1,2-peroxo-Fe2(III/III), the substrate hydrogen abstraction by Fe(IV)=O, and the hydroxyl rebound to the substrate N radical. The stochastic addition of H+/e- to the FeB side (mechanism C) can transition to mechanism B, thereby preventing enzyme deactivation. Two other competing mechanisms, involving the direct O-O bond dissociation (mechanism A) and the addition of H2O as a co-substrate (mechanism D), have been ruled out. SznF, a member of the emerging family of heme-oxygenase-like (HO-like) di-iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion of N -methyl-L-arginine (L-NMA) into N-nitroso-containing product, which can subsequently be transformed into streptozotocin. Using unrestricted density functional theory (UDFT) with the hybrid functional B3LYP, we have mechanistically investigated the two sequential hydroxylations of L-NMA catalyzed by SznF's binuclear iron central domain. Mechanism B primarily involves the O-O bond dissociation, forming Fe(IV)=O, induced by the H /e introduction to the Fe side of μ-1,2-peroxo-Fe (III/III), the substrate hydrogen abstraction by Fe(IV)=O, and the hydroxyl rebound to the substrate N radical. The stochastic addition of H /e to the Fe side (mechanism C) can transition to mechanism B, thereby preventing enzyme deactivation. Two other competing mechanisms, involving the direct O-O bond dissociation (mechanism A) and the addition of H O as a co-substrate (mechanism D), have been ruled out. SznF, a member of the emerging family of heme‐oxygenase‐like (HO‐like) di‐iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion of Nω‐methyl‐L‐arginine (L‐NMA) into N‐nitroso‐containing product, which can subsequently be transformed into streptozotocin. Using unrestricted density functional theory (UDFT) with the hybrid functional B3LYP, we have mechanistically investigated the two sequential hydroxylations of L‐NMA catalyzed by SznF's binuclear iron central domain. Mechanism B primarily involves the O−O bond dissociation, forming Fe(IV)=O, induced by the H+/e− introduction to the FeA side of μ‐1,2‐peroxo‐Fe2(III/III), the substrate hydrogen ion by Fe(IV)=O, and the hydroxyl rebound to the substrate N radical. The stochastic addition of H+/e− to the FeB side (mechanism C) can transition to mechanism B, thereby preventing enzyme deactivation. Two other competing mechanisms, involving the direct O−O bond dissociation (mechanism A) and the addition of H2O as a co‐substrate (mechanism D), have been ruled out. Enzyme catalysis: The consecutive hydroxylation mechanism of Nω‐methyl‐L‐arginine (L‐NMA) catalyzed by SznF's di‐iron domain is presented. Initiated by the peroxo‐Fe2(III/III) intermediate, the reaction involves proton/electron (H+/e−) addition on either side of this intermediate facilitating the generation of Nδ‐hydroxy‐Nω‐methyl‐L‐arginine (L‐HMA) and Nδ‐hydroxy‐Nω‐hydroxy‐Nω‐methyl‐L‐arginine (L–DHMA). |
Author | Chen, Shi‐Lu Li, Rui‐Ning |
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Keywords | di-iron cluster SznF density functional calculations streptozotocin N-hydroxylation |
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Snippet | SznF, a member of the emerging family of heme‐oxygenase‐like (HO‐like) di‐iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion... SznF, a member of the emerging family of heme-oxygenase-like (HO-like) di-iron oxidases and oxygenases, employs two distinct domains to catalyze the conversion... Abstract SznF, a member of the emerging family of heme‐oxygenase‐like (HO‐like) di‐iron oxidases and oxygenases, employs two distinct domains to catalyze the... |
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SubjectTerms | Catalysis density functional calculations Density functional theory di-iron cluster Hydroxylation Iron Iron - chemistry N-hydroxylation Oxygenases - chemistry Stochasticity Streptozocin streptozotocin Substrates SznF |
Title | Mechanistic Insights into the N‐Hydroxylations Catalyzed by the Binuclear Iron Domain of SznF Enzyme: Key Piece in the Synthesis of Streptozotocin |
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