Spectroscopic and Electronic Structure Description of the Reduced Binuclear Non-Heme Iron Active Site in Ribonucleotide Reductase fromE.coli:  Comparison to Reduced Δ9Desaturase and Electronic Structure Contributions to Differences in O2Reactivity

2000 ◽  
Vol 122 (35) ◽  
pp. 8495-8510 ◽  
Author(s):  
Yi-Shan Yang ◽  
Jeffrey Baldwin ◽  
Brenda A. Ley ◽  
J. Martin Bollinger, ◽  
Edward I. Solomon
Keyword(s):  
Electronic Structure ◽  
Ribonucleotide Reductase ◽  
Active Site ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Structure Description

scholarly journals Geometric and Electronic Structure of the Mn(IV)Fe(III) Cofactor in Class Ic Ribonucleotide Reductase: Correlation to the Class Ia Binuclear Non-Heme Iron Enzyme

2013 ◽  
Vol 135 (46) ◽  
pp. 17573-17584 ◽  
Author(s):  
Yeonju Kwak ◽  
Wei Jiang ◽  
Laura M. K. Dassama ◽  
Kiyoung Park ◽  
Caleb B. Bell ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Ribonucleotide Reductase ◽  
Heme Iron ◽  
Non Heme Iron

scholarly journals Spectroscopy of Non-Heme Iron Thiolate Complexes:  Insight into the Electronic Structure of the Low-Spin Active Site of Nitrile Hydratase

2005 ◽  
Vol 44 (6) ◽  
pp. 1826-1836 ◽  
Author(s):  
Pierre Kennepohl ◽  
Frank Neese ◽  
Dirk Schweitzer ◽  
Henry L. Jackson ◽  
Julie A. Kovacs ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Active Site ◽  
Nitrile Hydratase ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Thiolate Complexes ◽  
Iron Thiolate ◽  
Insight Into

Spectroscopic Definition of the Geometric and Electronic Structure of the Non-Heme Iron Active Site in Iron(II) Bleomycin: Correlation with Oxygen Reactivity

1995 ◽  
Vol 117 (16) ◽  
pp. 4545-4561 ◽  
Author(s):  
Kelly E. Loeb ◽  
Jeffrey M. Zaleski ◽  
Tami E. Westre ◽  
Richard J. Guajardo ◽  
Pradip K. Mascharak ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Active Site ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Definition Of ◽  
Oxygen Reactivity

scholarly journals Sulfur K-Edge XAS and DFT Calculations on Nitrile Hydratase:  Geometric and Electronic Structure of the Non-heme Iron Active Site

2006 ◽  
Vol 128 (2) ◽  
pp. 533-541 ◽  
Author(s):  
Abhishek Dey ◽  
Marina Chow ◽  
Kayoko Taniguchi ◽  
Priscilla Lugo-Mas ◽  
Steven Davin ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Dft Calculations ◽  
Active Site ◽  
Nitrile Hydratase ◽  
Heme Iron ◽  
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.

Peroxo-Type Intermediates in Class I Ribonucleotide Reductase and Related Binuclear Non-Heme Iron Enzymes

2009 ◽  
Vol 131 (34) ◽  
pp. 12155-12171 ◽  
Author(s):  
Kasper P. Jensen ◽  
Caleb B. Bell, ◽  
Michael D. Clay ◽  
Edward I. Solomon
Keyword(s):  
Ribonucleotide Reductase ◽  
Heme Iron ◽  
Class I ◽  
Non Heme Iron ◽  
Iron Enzymes

ChemInform Abstract: Geometric and Electronic Structure/Function Correlations in Non-heme Iron Enzymes

ChemInform ◽  
2010 ◽  
Vol 31 (13) ◽  
pp. no-no
Author(s):  
Edward I. Solomon ◽  
Thomas C. Brunold ◽  
Mindy I. Davis ◽  
Jyllian N. Kemsley ◽  
Sang-Kyu Lee ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Structure Function ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Iron Enzymes

scholarly journals Geometric and Electronic Structure Contributions to Function in Non-heme Iron Enzymes

2013 ◽  
Vol 46 (11) ◽  
pp. 2725-2739 ◽  
Author(s):  
Edward I. Solomon ◽  
Kenneth M. Light ◽  
Lei V. Liu ◽  
Martin Srnec ◽  
Shaun D. Wong
Keyword(s):  
Electronic Structure ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Iron Enzymes

The Molecular and Electronic Structure of Symmetrically and Asymmetrically Coordinated, Non-Heme Iron Complexes Containing [FeIII(μ-N)FeIV]4+ (S=3/2) and [FeIV(μ-N)FeIV]5+ (S=0) Cores

1999 ◽  
Vol 5 (2) ◽  
pp. 793-810 ◽  
Author(s):  
Thomas Jüstel ◽  
Michael Müller ◽  
Thomas Weyhermüller ◽  
Claudia Kressl ◽  
Eckhard Bill ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Iron Complexes ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Molecular And Electronic Structure
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