Oxygen Activation by Rieske Non-Heme Iron Oxygenases, a Theoretical Insight

2004 ◽  
Vol 108 (34) ◽  
pp. 13031-13041 ◽  
Author(s):  
Arianna Bassan ◽  
Margareta R. A. Blomberg ◽  
Tomasz Borowski ◽  
Per E. M. Siegbahn
Keyword(s):  
Oxygen Activation ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Theoretical Insight

Theoretical studies of oxygen activation by non-heme iron enzymes

2003 ◽  
Vol 96 (1) ◽  
pp. 62
Author(s):  
Arianna Bassan ◽  
Margareta R.A. Blomberg ◽  
Per E.M. Siegbahn
Keyword(s):  
Oxygen Activation ◽  
Heme Iron ◽  
Theoretical Studies ◽  
Non Heme Iron ◽  
Iron Enzymes

Oxygen Activation by Mononuclear Non-Heme Iron Proteins

1996 ◽  
Vol 35 (6) ◽  
pp. 609-611 ◽  
Author(s):  
Alexandre L. Nivorozhkin ◽  
Jean-Jacques Girerd
Keyword(s):  
Oxygen Activation ◽  
Heme Iron ◽  
Iron Proteins ◽  
Non Heme Iron

Structural Features That Control Oxygen Activation at the Non-Heme Iron Site in Fe(II)-Bleomycin: An Analog Study

1995 ◽  
Vol 117 (13) ◽  
pp. 3883-3884 ◽  
Author(s):  
Richard J. Guajardo ◽  
Ferman Chavez ◽  
Edgardo T. Farinas ◽  
Pradip K. Mascharak
Keyword(s):  
Oxygen Activation ◽  
Structural Features ◽  
Heme Iron ◽  
Iron Site ◽  
Non Heme Iron ◽  
Analog Study

[Fe(PMA)]n+ (n = 1,2): good models of iron-bleomycins and examples of mononuclear non-heme iron complexes with significant oxygen-activation capabilities

1993 ◽  
Vol 115 (18) ◽  
pp. 7971-7977 ◽  
Author(s):  
Richard J. Guajardo ◽  
Samuel E. Hudson ◽  
Steven J. Brown ◽  
Pradip K. Mascharak
Keyword(s):  
Oxygen Activation ◽  
Iron Complexes ◽  
Heme Iron ◽  
Non Heme Iron

Post-translational self-hydroxylation: A probe for oxygen activation mechanisms in non-heme iron enzymes

2005 ◽  
Vol 338 (1) ◽  
pp. 230-239 ◽  
Author(s):  
Erik R. Farquhar ◽  
Kevin D. Koehntop ◽  
Joseph P. Emerson ◽  
Lawrence Que
Keyword(s):  
Oxygen Activation ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Iron Enzymes ◽  
Activation Mechanisms

ChemInform Abstract: Oxygen Activation by Mononuclear Non-Heme Iron Proteins

ChemInform ◽  
2010 ◽  
Vol 27 (28) ◽  
pp. no-no
Author(s):  
A. L. NIVOROZHKIN ◽  
J.-J. GIRERD
Keyword(s):  
Oxygen Activation ◽  
Heme Iron ◽  
Iron Proteins ◽  
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.

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