Characteristic Effect of Pyridine on the NIH Shift and Selectivity in the Monooxygenation of Aromatic Compounds Catalyzed by a Nonheme Iron Complex/Hydroquinones/O2System

1992 ◽  
Vol 21 (7) ◽  
pp. 1279-1282 ◽  
Author(s):  
Takuzo Funabiki ◽  
Takehiro Toyoda ◽  
Satohiro Yoshida
Keyword(s):  
Aromatic Compounds ◽  
Iron Complex ◽  
Nonheme Iron ◽  
Characteristic Effect

Bioinspired Olefin cis-Dihydroxylation and Aliphatic C–H Bond Hydroxylation with Dioxygen Catalyzed by a Nonheme Iron Complex

2018 ◽  
Vol 57 (16) ◽  
pp. 10160-10169 ◽  
Author(s):  
Sayanti Chatterjee ◽  
Shrabanti Bhattacharya ◽  
Tapan Kanti Paine
Keyword(s):  
Iron Complex ◽  
Nonheme Iron

Dinitrosyliron Complex [(PMDTA)Fe(NO)2]: Intermediate for Nitric Oxide Monooxygenation Activity in Nonheme Iron Complex

2020 ◽  
Vol 59 (12) ◽  
pp. 8308-8319
Author(s):  
Shan Lu ◽  
Tzung-Wen Chiou ◽  
Wei-Liang Li ◽  
Chun-Chieh Wang ◽  
Yun-Ming Wang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Iron Complex ◽  
Nonheme Iron

scholarly journals Mechanistic Investigation of Oxygen Rebound in a Mononuclear Nonheme Iron Complex

2019 ◽  
Vol 58 (15) ◽  
pp. 9557-9561 ◽  
Author(s):  
Thomas M. Pangia ◽  
Vishal Yadav ◽  
Emilie F. Gérard ◽  
Yen-Ting Lin ◽  
Sam P. de Visser ◽  
...  
Keyword(s):  
Iron Complex ◽  
Nonheme Iron ◽  
Mechanistic Investigation

Shape-Selective Interception by Hydrocarbons of the O2-Derived Oxidant of a Biomimetic Nonheme Iron Complex

2009 ◽  
Vol 121 (10) ◽  
pp. 1812-1815 ◽  
Author(s):  
Anusree Mukherjee ◽  
Marlène Martinho ◽  
Emile L. Bominaar ◽  
Eckard Münck ◽  
Lawrence Que
Keyword(s):  
Iron Complex ◽  
Nonheme Iron ◽  
Shape Selective

Nonheme iron complex-catalyzed efficient alcohol oxidation by t-BuOOH with N-hydroxyphthalimide (NHPI) as co-catalyst: Implication of high valent iron-oxo species

2016 ◽  
Vol 451 ◽  
pp. 8-15 ◽  
Author(s):  
Jeong Mi Bae ◽  
Myoung Mi Lee ◽  
Seul Ah Lee ◽  
Sun Young Lee ◽  
Kwon Hee Bok ◽  
...  
Keyword(s):  
Alcohol Oxidation ◽  
Iron Complex ◽  
Nonheme Iron ◽  
Co Catalyst ◽  
High Valent

Unusual efficiency of a non-heme iron complex as catalyst for the hydroxylation of aromatic compounds by hydrogen peroxide: comparison with iron porphyrins

2002 ◽  
Vol 5 (4) ◽  
pp. 263-266 ◽  
Author(s):  
Jean-François Bartoli ◽  
François Lambert ◽  
Irène Morgenstern-Badarau ◽  
Pierrette Battioni ◽  
Daniel Mansuy
Keyword(s):  
Hydrogen Peroxide ◽  
Aromatic Compounds ◽  
Iron Complex ◽  
Heme Iron ◽  
Iron Porphyrins ◽  
Non Heme Iron

scholarly journals Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases

2021 ◽  
Vol 87 (6) ◽  
Author(s):  
Yan-Jie Hou ◽  
Yuan Guo ◽  
De-Feng Li ◽  
Ning-Yi Zhou
Keyword(s):  
Aromatic Compounds ◽  
Substrate Binding ◽  
Large Subunit ◽  
Binding Pocket ◽  
Small Subunit ◽  
Nonheme Iron ◽  
Hydroxyl Groups ◽  
Substrate Protein ◽  
Aromatic Compound Degradation ◽  
Polycyclic Aromatic

ABSTRACT Rieske nonheme iron oxygenases (ROs) catalyze the oxidation of a wide variety of substrates and play important roles in aromatic compound degradation and polycyclic aromatic hydrocarbon degradation. Those Rieske dioxygenases that usually act on hydrophobic substrates have been extensively studied and structurally characterized. Here, we report the crystal structure of a novel Rieske monooxygenase, NagGH, the oxygenase component of a salicylate 5-monooxygenase from Ralstonia sp. strain U2 that catalyzes the hydroxylation of a hydrophilic substrate salicylate (2-hydroxybenzoate), forming gentisate (2, 5-dihydroxybenzoate). The large subunit NagG and small subunit NagH share the same fold as that for their counterparts of Rieske dioxygenases and assemble the same α3β3 hexamer, despite that they share low (or no identity for NagH) sequence identities with these dioxygenase counterparts. A potential substrate-binding pocket was observed in the vicinity of the nonheme iron site. It featured a positively charged residue Arg323 that was surrounded by hydrophobic residues. The shift of nonheme iron atom caused by residue Leu228 disrupted the usual substrate pocket observed in other ROs. Residue Asn218 at the usual substrate pocket observed in other ROs was likewise involved in substrate binding and oxidation, yet residues Gln316 and Ser367, away from the usual substrate pocket of other ROs, were shown to play a more important role in substrate oxidation than Asn218. The unique binding pocket and unusual substrate-protein hydrophilic interaction provide new insights into Rieske monooxygenases. IMPORTANCE Rieske oxygenases are involved in the degradation of various aromatic compounds. These dioxygenases usually carry out hydroxylation of hydrophobic aromatic compounds and supply substrates with hydroxyl groups for extradiol/intradiol dioxygenases to cleave rings, and have been extensively studied. Salicylate 5-hydroxylase NagGH is a novel Rieske monooxygenase with high similarity to Rieske dioxygenases, and also shares reductase and ferredoxin similarity with a Rieske dioxygenase naphthalene 1,2-dioxygenase (NagAcAd) in Ralstonia sp. strain U2. The structure of NagGH, the oxygenase component of salicylate 5-monooxygenase, gives a representative of those monooxygenases and will help us understand the mechanism of their substrate binding and product regio-selectivity.

scholarly journals Catalytic Alkyl Hydroperoxide and Acyl Hydroperoxide Disproportionation by a Nonheme Iron Complex

ACS Catalysis ◽  
2018 ◽  
Vol 8 (11) ◽  
pp. 9980-9991 ◽  
Author(s):  
Christina Wegeberg ◽  
Wesley R. Browne ◽  
Christine J. McKenzie
Keyword(s):  
Iron Complex ◽  
Nonheme Iron ◽  
Alkyl Hydroperoxide
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