Direct reactivity studies of non-heme iron-oxo intermediates toward alkane oxidation

2018 ◽  
Vol 108 ◽  
pp. 77-81 ◽  
Author(s):  
Alexandra M. Zima ◽  
Oleg Y. Lyakin ◽  
Konstantin P. Bryliakov ◽  
Evgenii P. Talsi
Keyword(s):  
Heme Iron ◽  
Alkane Oxidation ◽  
Non Heme Iron

[FeIII(PMA)]2+:  A Mononuclear Non-Heme Iron Complex That Catalyzes Alkane Oxidation

1996 ◽  
Vol 35 (21) ◽  
pp. 6273-6281 ◽  
Author(s):  
Cattien Nguyen ◽  
Richard J. Guajardo ◽  
Pradip K. Mascharak
Keyword(s):  
Iron Complex ◽  
Heme Iron ◽  
Alkane Oxidation ◽  
Non Heme Iron

scholarly journals Unraveling the origins of catalyst degradation in non-heme iron-based alkane oxidation

2014 ◽  
Vol 43 (45) ◽  
pp. 17108-17119 ◽  
Author(s):  
Michaela Grau ◽  
Andrew Kyriacou ◽  
Fernando Cabedo Martinez ◽  
Irene M. de Wispelaere ◽  
Andrew J. P. White ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Heme Iron ◽  
Alkane Oxidation ◽  
Non Heme Iron ◽  
Amine Ligands ◽  
Iron Based

A series of iron(ii) complexes with tetradentate and pentadentate pyridyl amine ligands has been used for the oxidation of cyclohexane with hydrogen peroxide. Ligand degradation is observed under oxidising conditions via oxidative N-dealkylation.

scholarly journals Steric Modifications Tune the Regioselectivity of the Alkane Oxidation Catalyzed by Non-Heme Iron Complexes

2012 ◽  
Vol 51 (13) ◽  
pp. 7431-7431 ◽  
Author(s):  
Yu He ◽  
John D. Gorden ◽  
Christian R. Goldsmith
Keyword(s):  
Iron Complexes ◽  
Heme Iron ◽  
Alkane Oxidation ◽  
Non Heme Iron

Towards robust alkane oxidation catalysts: electronic variations in non-heme iron(ii) complexes and their effect in catalytic alkane oxidation

2009 ◽  
pp. 5319 ◽  
Author(s):  
Jason England ◽  
Reema Gondhia ◽  
Laura Bigorra-Lopez ◽  
Allan R. Petersen ◽  
Andrew J. P. White ◽  
...  
Keyword(s):  
Heme Iron ◽  
Alkane Oxidation ◽  
Oxidation Catalysts ◽  
Non Heme Iron

scholarly journals Steric Modifications Tune the Regioselectivity of the Alkane Oxidation Catalyzed by Non-Heme Iron Complexes

2011 ◽  
Vol 50 (24) ◽  
pp. 12651-12660 ◽  
Author(s):  
Yu He ◽  
John D. Gorden ◽  
Christian R. Goldsmith
Keyword(s):  
Iron Complexes ◽  
Heme Iron ◽  
Alkane Oxidation ◽  
Non Heme Iron

Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD

2019 ◽  
Author(s):  
Christopher John ◽  
Greg M. Swain ◽  
Robert P. Hausinger ◽  
Denis A. Proshlyakov
Keyword(s):  
Active Site ◽  
Structural Model ◽  
Heme Iron ◽  
Chemical Transformations ◽  
Experimental Conditions ◽  
Strongly Coupled ◽  
Non Heme Iron ◽  
Reversible Redox ◽  
Wide Range ◽  
Complex Structural

2-Oxoglutarate (2OG)-dependent dioxygenases catalyze C-H activation while performing a wide range of chemical transformations. In contrast to their heme analogues, non-heme iron centers afford greater structural flexibility with important implications for their diverse catalytic mechanisms. We characterize an <i>in situ</i> structural model of the putative transient ferric intermediate of 2OG:taurine dioxygenase (TauD) by using a combination of spectroelectrochemical and semi-empirical computational methods, demonstrating that the Fe (III/II) transition involves a substantial, fully reversible, redox-linked conformational change at the active site. This rearrangement alters the apparent redox potential of the active site between -127 mV for reduction of the ferric state and 171 mV for oxidation of the ferrous state of the 2OG-Fe-TauD complex. Structural perturbations exhibit limited sensitivity to mediator concentrations and potential pulse duration. Similar changes were observed in the Fe-TauD and taurine-2OG-Fe-TauD complexes, thus attributing the reorganization to the protein moiety rather than the cosubstrates. Redox difference infrared spectra indicate a reorganization of the protein backbone in addition to the involvement of carboxylate and histidine ligands. Quantitative modeling of the transient redox response using two alternative reaction schemes across a variety of experimental conditions strongly supports the proposal for intrinsic protein reorganization as the origin of the experimental observations.

Plant carotenoid cleavage oxygenases: structure–function relationships and role in development and metabolism

2019 ◽  
Vol 19 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Manoj Kumar Dhar ◽  
Sonal Mishra ◽  
Archana Bhat ◽  
Sudha Chib ◽  
Sanjana Kaul
Keyword(s):  
Higher Plants ◽  
Domain Architecture ◽  
Heme Iron ◽  
Critical Assessment ◽  
Protein Family ◽  
Regulatory Mechanisms ◽  
Non Heme Iron ◽  
Functional Aspects ◽  
Functional Understanding ◽  
Signal Production

Abstract A plant communicates within itself and with the outside world by deploying an array of agents that include several attractants by virtue of their color and smell. In this category, the contribution of ‘carotenoids and apocarotenoids’ is very significant. Apocarotenoids, the carotenoid-derived compounds, show wide representation among organisms. Their biosynthesis occurs by oxidative cleavage of carotenoids, a high-value reaction, mediated by carotenoid cleavage oxygenases or carotenoid cleavage dioxygenases (CCDs)—a family of non-heme iron enzymes. Structurally, this protein family displays wide diversity but is limited in its distribution among plants. Functionally, this protein family has been recognized to offer a role in phytohormones, volatiles and signal production. Further, their wide presence and clade-specific functional disparity demands a comprehensive account. This review focuses on the critical assessment of CCDs of higher plants, describing recent progress in their functional aspects and regulatory mechanisms, domain architecture, classification and localization. The work also highlights the relevant discussion for further exploration of this multi-prospective protein family for the betterment of its functional understanding and improvement of crops.

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