scholarly journals Spectroscopic and Electronic Structure Study of ETHE1: Elucidating the Factors Influencing Sulfur Oxidation and Oxygenation in Mononuclear Nonheme Iron Enzymes

2018 ◽  
Vol 140 (44) ◽  
pp. 14887-14902 ◽  
Author(s):  
Serra Goudarzi ◽  
Jeffrey T. Babicz ◽  
Omer Kabil ◽  
Ruma Banerjee ◽  
Edward I. Solomon
Keyword(s):  
Electronic Structure ◽  
Sulfur Oxidation ◽  
Structure Study ◽  
Nonheme Iron ◽  
Nonheme Iron Enzymes ◽  
Factors Influencing ◽  
Iron Enzymes

scholarly journals Direct coordination of pterin to FeII enables neurotransmitter biosynthesis in the pterin-dependent hydroxylases

2021 ◽  
Vol 118 (15) ◽  
pp. e2022379118
Author(s):  
Shyam R. Iyer ◽  
Kasper D. Tidemand ◽  
Jeffrey T. Babicz ◽  
Ariel B. Jacobs ◽  
Leland B. Gee ◽  
...  
Keyword(s):  
Active Site ◽  
Tryptophan Hydroxylase ◽  
Activation Barrier ◽  
Magnetic Circular Dichroism ◽  
Aromatic Amino Acids ◽  
Oxygen Activation ◽  
Nonheme Iron ◽  
Nonheme Iron Enzymes ◽  
Iron Enzymes ◽  
Pterin Cofactor

The pterin-dependent nonheme iron enzymes hydroxylate aromatic amino acids to perform the biosynthesis of neurotransmitters to maintain proper brain function. These enzymes activate oxygen using a pterin cofactor and an aromatic amino acid substrate bound to the FeII active site to form a highly reactive FeIV = O species that initiates substrate oxidation. In this study, using tryptophan hydroxylase, we have kinetically generated a pre-FeIV = O intermediate and characterized its structure as a FeII-peroxy-pterin species using absorption, Mössbauer, resonance Raman, and nuclear resonance vibrational spectroscopies. From parallel characterization of the pterin cofactor and tryptophan substrate–bound ternary FeII active site before the O2 reaction (including magnetic circular dichroism spectroscopy), these studies both experimentally define the mechanism of FeIV = O formation and demonstrate that the carbonyl functional group on the pterin is directly coordinated to the FeII site in both the ternary complex and the peroxo intermediate. Reaction coordinate calculations predict a 14 kcal/mol reduction in the oxygen activation barrier due to the direct binding of the pterin carbonyl to the FeII site, as this interaction provides an orbital pathway for efficient electron transfer from the pterin cofactor to the iron center. This direct coordination of the pterin cofactor enables the biological function of the pterin-dependent hydroxylases and demonstrates a unified mechanism for oxygen activation by the cofactor-dependent nonheme iron enzymes.

A Model forα-Keto Acid Dependent Nonheme Iron Enzymes: Structure and Reactivity of[Fe2II(Me2hdp)2(bf)](ClO4)

1994 ◽  
Vol 33 (18) ◽  
pp. 1886-1888 ◽  
Author(s):  
Yu-Min Chiou ◽  
Lawrence Que
Keyword(s):  
Nonheme Iron ◽  
Keto Acid ◽  
Nonheme Iron Enzymes ◽  
Iron Enzymes

Functional models for mononuclear nonheme iron enzymes

2003 ◽  
Vol 7 (6) ◽  
pp. 674-682 ◽  
Author(s):  
J Rohde
Keyword(s):  
Nonheme Iron ◽  
Nonheme Iron Enzymes ◽  
Iron Enzymes ◽  
Functional Models

Models for Amide Ligation in Nonheme Iron Enzymes

1997 ◽  
Vol 36 (24) ◽  
pp. 5424-5425 ◽  
Author(s):  
Sanjay K. Mandal ◽  
Lawrence Que
Keyword(s):  
Nonheme Iron ◽  
Nonheme Iron Enzymes ◽  
Iron Enzymes

scholarly journals Peroxo and oxo intermediates in mononuclear nonheme iron enzymes and related active sites

2009 ◽  
Vol 13 (1) ◽  
pp. 99-113 ◽  
Author(s):  
Edward I Solomon ◽  
Shaun D Wong ◽  
Lei V Liu ◽  
Andrea Decker ◽  
Marina S Chow
Keyword(s):  
Active Sites ◽  
Nonheme Iron ◽  
Nonheme Iron Enzymes ◽  
Iron Enzymes

scholarly journals On the ligand field of iron in ferredoxin from spinach chloroplasts and related nonheme iron enzymes.

1966 ◽  
Vol 55 (2) ◽  
pp. 397-404 ◽  
Author(s):  
H. Brintzinger ◽  
G. Palmer ◽  
R. H. Sands
Keyword(s):  
Nonheme Iron ◽  
Ligand Field ◽  
Nonheme Iron Enzymes ◽  
Spinach Chloroplasts ◽  
Iron Enzymes

scholarly journals Modeling nuclear resonance vibrational spectroscopic data of binuclear nonheme iron enzymes using density functional theory

2014 ◽  
Vol 92 (10) ◽  
pp. 975-978 ◽  
Author(s):  
Kiyoung Park ◽  
Edward I. Solomon
Keyword(s):  
Density Functional Theory ◽  
Active Sites ◽  
Density Functional ◽  
Structural Information ◽  
Nonheme Iron ◽  
Nuclear Resonance ◽  
Functional Theory ◽  
Nonheme Iron Enzymes ◽  
Iron Enzymes ◽  
Dft Model

Nuclear resonance vibrational spectroscopy (NRVS) is a powerful technique that can provide geometric structural information on key reaction intermediates of Fe-containing systems when utilized in combination with density functional theory (DFT). However, in the case of binuclear nonheme iron enzymes, DFT-predicted NRVS spectra have been found to be sensitive to the truncation method used to model the active sites of the enzymes. Therefore, in this study various-level truncation schemes have been tested to predict the NRVS spectrum of a binuclear nonheme iron enzyme, and a reasonably sized DFT model that is suitable for employing the NRVS/DFT combined methodology to characterize binuclear nonheme iron enzymes has been developed.

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