Reversible C–C Bond Formation between Redox-Active Pyridine Ligands in Iron Complexes

2012 ◽  
Vol 134 (50) ◽  
pp. 20352-20364 ◽  
Author(s):  
Thomas R. Dugan ◽  
Eckhard Bill ◽  
K. Cory MacLeod ◽  
Gemma J. Christian ◽  
Ryan E. Cowley ◽  
...  
Keyword(s):  
Bond Formation ◽  
Iron Complexes ◽  
Pyridine Ligands ◽  
Redox Active

scholarly journals Bioelectrocatalytic cofactor regeneration coupled to CO2 fixation in a redox‐active hydrogel for stereoselective C‐C bond formation

2021 ◽  
Author(s):  
Leonardo Castañeda-Losada ◽  
David Adam ◽  
Nicole Paczia ◽  
Darren Buesen ◽  
Fabian Steffler ◽  
...  
Keyword(s):  
Co2 Fixation ◽  
Bond Formation ◽  
Cofactor Regeneration ◽  
Redox Active

scholarly journals Bioelectrocatalytic Cofactor Regeneration Coupled to CO 2 Fixation in a Redox‐Active Hydrogel for Stereoselective C−C Bond Formation

2021 ◽  
Author(s):  
Leonardo Castañeda‐Losada ◽  
David Adam ◽  
Nicole Paczia ◽  
Darren Buesen ◽  
Fabian Steffler ◽  
...  
Keyword(s):  
Bond Formation ◽  
Cofactor Regeneration ◽  
Redox Active

scholarly journals The ArcB Sensor Kinase of Escherichia coli Autophosphorylates by an Intramolecular Reaction

2010 ◽  
Vol 192 (6) ◽  
pp. 1735-1739 ◽  
Author(s):  
Gabriela R. Peña-Sandoval ◽  
Dimitris Georgellis
Keyword(s):  
Response Regulator ◽  
Bond Formation ◽  
Sensor Kinase ◽  
Two Component System ◽  
Histidine Kinases ◽  
Intramolecular Reaction ◽  
Redox Active ◽  
Intermolecular Disulfide Bond ◽  
Two Component ◽  
Respiratory Conditions

ABSTRACT The Arc two-component system, comprising the ArcB sensor kinase and the ArcA response regulator, modulates the expression of numerous genes in response to the respiratory conditions of growth. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here we show that ArcB autophosphorylates through an intramolecular reaction which diverges from the usually envisaged intermolecular autophosphorylation of homodimeric histidine kinases.

Synthesis and Catalysis of Redox-Active Bis(imino)acenaphthene (BIAN) Iron Complexes

ChemCatChem ◽  
2017 ◽  
Vol 9 (16) ◽  
pp. 3203-3209 ◽  
Author(s):  
Matteo Villa ◽  
Dominique Miesel ◽  
Alexander Hildebrandt ◽  
Fabio Ragaini ◽  
Dieter Schaarschmidt ◽  
...  
Keyword(s):  
Iron Complexes ◽  
Redox Active

Galectin-13/placental protein 13: redox-active disulfides as switches for regulating structure, function and cellular distribution

Glycobiology ◽  
2019 ◽  
Vol 30 (2) ◽  
pp. 120-129 ◽  
Author(s):  
Tong Yang ◽  
Yuan Yao ◽  
Xing Wang ◽  
Yuying Li ◽  
Yunlong Si ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Bond Formation ◽  
Gel Filtration ◽  
Wild Type ◽  
High Concentration ◽  
Redox Active ◽  
Placental Protein ◽  
The Relationship ◽  
Low Expression

Abstract Galectin-13 (Gal-13) plays numerous roles in regulating the relationship between maternal and fetal tissues. Low expression levels or mutations of the lectin can result in pre-eclampsia. The previous crystal structure and gel filtration data show that Gal-13 dimerizes via formation of two disulfide bonds formed by Cys136 and Cys138. In the present study, we mutated them to serine (C136S, C138S and C136S/C138S), crystalized the variants and solved their crystal structures. All variants crystallized as monomers. In the C136S structure, Cys138 formed a disulfide bond with Cys19, indicating that Cys19 is important for regulation of reversible disulfide bond formation in this lectin. Hemagglutination assays demonstrated that all variants are inactive at inducing erythrocyte agglutination, even though gel filtration profiles indicate that C136S and C138S could still form dimers, suggesting that these dimers do not exhibit the same activity as wild-type (WT) Gal-13. In HeLa cells, the three variants were found to be distributed the same as with WT Gal-13. However, a Gal-13 variant (delT221) truncated at T221 could not be transported into the nucleus, possibly explaining why women having this variant get pre-eclampsia. Considering the normally high concentration of glutathione in cells, WT Gal-13 should exist mostly as a monomer in cytoplasm, consistent with the monomeric variant C136S/C138S, which has a similar ability to interact with HOXA1 as WT Gal-13.

scholarly journals Zn-Templated synthesis of substituted (2,6-diimine)pyridine proligands and evaluation of their iron complexes as anolytes for flow battery applications

2020 ◽  
Vol 49 (45) ◽  
pp. 16175-16183 ◽  
Author(s):  
Jason D. Braun ◽  
Paul A. Gray ◽  
Baldeep K. Sidhu ◽  
Dion B. Nemez ◽  
David E. Herbert
Keyword(s):  
Iron Complexes ◽  
Flow Battery ◽  
Strong Electron ◽  
Templated Synthesis ◽  
Redox Flow Batteries ◽  
Pyridine Ligands ◽  
Flow Batteries ◽  
Multiple Ligand

Zn2+ templating enables synthesis of redox ‘non-innocent’ diimine pyridine ligands with strong electron-withdrawing groups, allowing construction of iron complexes with multiple ligand-based reductions for application in redox flow batteries.

Photocatalytic redox reactions with metalloporphyrins

2020 ◽  
Vol 24 (01n03) ◽  
pp. 21-32 ◽  
Author(s):  
Shunichi Fukuzumi ◽  
Yong-Min Lee ◽  
Wonwoo Nam
Keyword(s):  
Hydrogen Evolution ◽  
Redox Reactions ◽  
Bond Formation ◽  
Visible Region ◽  
Photosynthetic Reaction Center ◽  
Structure And Function ◽  
Free Base ◽  
Redox Catalyst ◽  
Redox Active ◽  
And Function

Metalloporphyrinoids are utilized as efficient sensitizers and catalysts in photosynthesis and the reverse reaction that is respiration. Because metalloporphyrinoids show strong absorption in the visible region and redox active, metalloporphyrinoids are also suited as photoredox catalysts for photo-driven redox reactions using solar energy. In particular, metalloporphyrins are utilized as pivotal components to mimic the structure and function of the photosynthetic reaction center. Metalloporphyrins are used as photoredox catalysts for hydrogen evolution from electron and proton sources combining hydrogen evolution catalysts. Metalloporphyrins also act as thermal redox catalysts for photocatalytic reduction of CO2 with photoredox catalysts. Metalloporphyrins are also used as dual catalysts for a photoredox catalyst for oxygenation of substrates with H2O and a redox catalyst for O2 reduction when dioxygen is used as a two-electron oxidant and H2O as an oxygen source, both of which are the greenest reactants. Free base porphyrins can also be employed as promising photoredox catalysts for C–C bond formation reactions.

Activation of sp3Carbon−Hydrogen Bonds by Cobalt and Iron Complexes and Subsequent C−C Bond Formation

2009 ◽  
Vol 28 (20) ◽  
pp. 6090-6095 ◽  
Author(s):  
Guoqiang Xu ◽  
Hongjian Sun ◽  
Xiaoyan Li
Keyword(s):  
Hydrogen Bonds ◽  
Bond Formation ◽  
Iron Complexes
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