oxo-aquo-Mn(V)TM-4-pyridyl | 866594-21-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡啶及其衍生物
• 英文名称: oxo-aquo-Mn(V)TM-4-pyridyl
• CAS: 866594-21-0
• 化学式: C₄₄H₃₈MnN₈O₂
• 分子量: 765.776
• InChiKey: CBVGCPALKOHMQN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
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• 重原子数：
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• 可旋转键数：
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• 环数：
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• sp3杂化的碳原子比例：
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• 拓扑面积：
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• 氢给体数：
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• 氢受体数：
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反应信息

• 作为反应物：
  描述：

  oxo-aquo-Mn(V)TM-4-pyridyl 在 维生素 C 作用下， 以 水 为溶剂， 生成 [Mn(III)(TMpyP)(H2O)OH](4+)
  参考文献：
  名称：

  Manganese Porphyrins as Redox-Coupled Peroxynitrite Reductases

  摘要：

  Superoxide (O-2.(-)) and peroxynitrite (ONOO-) have been implicated in many pathophysiological conditions. To develop novel catalysts that have both ONOO- decomposition and O-2.(-) dismutase activity, and to understand the mechanisms of these processes, we have explored the reactivity of 5,10, 15,20-tetrakis(N-methyl-4'-pyridyl)porphinatomanganese [Mn(III)TMPyP] toward ONOO- and O-2.(-). The reaction of Mn(III)TMPyP with ONOO- to generate an oxomanganese(IV) porphyrin species [(oxoMn(IV)] is fast, but Mn(III)TMPyP is not catalytic for ONOO- decomposition because of the slow reduction of oxoMn(IV) back to the Mn(III) oxidation state. However, biological antioxidants such as ascorbate, glutathione, and Trolox rapidly turn over the catalytic cycle by reducing oxoMn(IV). Thus, Mn(III)TMPyP becomes an efficient peroxynitrite reductase when coupled with ascorbate, glutathione, and Trolox (k(c) approximate to 2 x 10(6) M-1 s(-1)), though the direct reactions of ONOO- with these biological antioxidants are slow (88 M-1 s(-1), 5.8 x 10(2) M-1 s(-1) and 33 M-1 s(-1), respectively). Mn(In)TMPyP is known to catalyze the dismutation of O-2.(-), and using stopped-flow spectrophotometry, the rate of Mn(III)TMPyP-catalyzed dismutation has been measured directly (k(c)= 1.1 x 10(7) M-1 s(-1)). Further, O-2.(-), like the biological antioxidants, rapidly reduces oxoMn(IV) to the Mn(III) oxidation state (k approximate to 10(8) M-1 s(-1)), transforming Mn(III)TMPyP into a O-2.(-)-coupled ONOO- reductase. Under conditions of oxidative stress and reduced antioxidant levels, Mn(III)TMPyP may deplete O-2.(-) primarily as a function of its ONOO- reductase activity, and not through its O-2.(-) dismutase activity.

  DOI：

  10.1021/ja9801036
• 作为产物：
  描述：

  亚硝酸氧盐 、 [Mn(III)(TMpyP)(H2O)OH](4+) 以 水 为溶剂， 生成 oxo-aquo-Mn(V)TM-4-pyridyl
  参考文献：
  名称：

  Manganese Porphyrins as Redox-Coupled Peroxynitrite Reductases

  摘要：

  Superoxide (O-2.(-)) and peroxynitrite (ONOO-) have been implicated in many pathophysiological conditions. To develop novel catalysts that have both ONOO- decomposition and O-2.(-) dismutase activity, and to understand the mechanisms of these processes, we have explored the reactivity of 5,10, 15,20-tetrakis(N-methyl-4'-pyridyl)porphinatomanganese [Mn(III)TMPyP] toward ONOO- and O-2.(-). The reaction of Mn(III)TMPyP with ONOO- to generate an oxomanganese(IV) porphyrin species [(oxoMn(IV)] is fast, but Mn(III)TMPyP is not catalytic for ONOO- decomposition because of the slow reduction of oxoMn(IV) back to the Mn(III) oxidation state. However, biological antioxidants such as ascorbate, glutathione, and Trolox rapidly turn over the catalytic cycle by reducing oxoMn(IV). Thus, Mn(III)TMPyP becomes an efficient peroxynitrite reductase when coupled with ascorbate, glutathione, and Trolox (k(c) approximate to 2 x 10(6) M-1 s(-1)), though the direct reactions of ONOO- with these biological antioxidants are slow (88 M-1 s(-1), 5.8 x 10(2) M-1 s(-1) and 33 M-1 s(-1), respectively). Mn(In)TMPyP is known to catalyze the dismutation of O-2.(-), and using stopped-flow spectrophotometry, the rate of Mn(III)TMPyP-catalyzed dismutation has been measured directly (k(c)= 1.1 x 10(7) M-1 s(-1)). Further, O-2.(-), like the biological antioxidants, rapidly reduces oxoMn(IV) to the Mn(III) oxidation state (k approximate to 10(8) M-1 s(-1)), transforming Mn(III)TMPyP into a O-2.(-)-coupled ONOO- reductase. Under conditions of oxidative stress and reduced antioxidant levels, Mn(III)TMPyP may deplete O-2.(-) primarily as a function of its ONOO- reductase activity, and not through its O-2.(-) dismutase activity.

  DOI：

  10.1021/ja9801036

文献信息

• Detection and Characterization of an Oxomanganese(V) Porphyrin Complex by Rapid-Mixing Stopped-Flow Spectrophotometry
  作者：John T. Groves、Jinbo Lee、Sudhakar S. Marla

  DOI：10.1021/ja962605u

  日期：1997.7.1

  The Soret maximum of 1 was found at 443 nm, intermediate between that of oxomanganese(IV) (428 nm) and Mn(III)TMPyP (462 nm), thus facilitating its detection. The rate of formation of 1 from Mn(III)TMPyP followed second-order kinetics, first order in Mn(III) porphyrin and first order in oxidant. The rate constants have the following order: m-CPBA (2.7 × 107 M-1 s-1) > HSO5- (6.9 × 105 M-1 s-1) ≈ ClO-

  描述了在环境催化条件下首次检测和表征氧锰 (V) 卟啉配合物。(四-(N-甲基吡啶基)卟啉基)锰(III) [Mn(III)TMPyP] 与多种氧化剂如间氯过氧苯甲酸 (m-CPBA)、HSO5- 和 ClO- 的反应已显示通过停流分光光度法生产相同的、短寿命的中间体 (1)。在 443 nm 处发现 Soret 最大值为 1，介于氧锰 (IV) (428 nm) 和 Mn (III) TMPyP (462 nm) 之间，从而促进其检测。从 Mn(III)TMPyP 形成 1 的速率遵循二级动力学，在 Mn(III) 卟啉中为一级，在氧化剂中为一级。速率常数具有以下顺序：m-CPBA (2.7 × 107 M-1 s-1) > HSO5- (6.9 × 105 M-1 s-1) ≈ ClO- (6.3 × 105 M-1 s-1) . 一旦形成，中间物种 1 通过单电子还原快速转化为 oxoMn(IV)