Effect of metal exchange (Os vs. Ru) and co-ligand variation (Cl−vs. acac−) on the oxidation state distribution in complexes of an o-phenylenediamido(2−)/o-quinonediimine redox system

2009 ◽  
pp. 7778 ◽  
Author(s):  
Sudipta Chatterjee ◽  
Priti Singh ◽  
Jan Fiedler ◽  
Radka Baková ◽  
Stanislav Záliš ◽  
...  
2009 ◽  
Vol 282 (3) ◽  
pp. 793-797 ◽  
Author(s):  
G. Lujanienė ◽  
J. Šapolaitė ◽  
E. Radžiūtė ◽  
V. Aninkevičius

2003 ◽  
Vol 125 (25) ◽  
pp. 7524-7525 ◽  
Author(s):  
Matthew D. Hall ◽  
Garry J. Foran ◽  
Mei Zhang ◽  
Philip J. Beale ◽  
Trevor W. Hambley

Chemosphere ◽  
2021 ◽  
Vol 274 ◽  
pp. 129741
Author(s):  
Nicole A. DiBlasi ◽  
Ezgi Yalçintas ◽  
Floyd E. Stanley ◽  
Donald T. Reed ◽  
Amy E. Hixon

2016 ◽  
Vol 113 (27) ◽  
pp. 7539-7544 ◽  
Author(s):  
David A. Hanna ◽  
Raven M. Harvey ◽  
Osiris Martinez-Guzman ◽  
Xiaojing Yuan ◽  
Bindu Chandrasekharan ◽  
...  

Heme is an essential cofactor and signaling molecule. Heme acquisition by proteins and heme signaling are ultimately reliant on the ability to mobilize labile heme (LH). However, the properties of LH pools, including concentration, oxidation state, distribution, speciation, and dynamics, are poorly understood. Herein, we elucidate the nature and dynamics of LH using genetically encoded ratiometric fluorescent heme sensors in the unicellular eukaryoteSaccharomyces cerevisiae. We find that the subcellular distribution of LH is heterogeneous; the cytosol maintains LH at ∼20–40 nM, whereas the mitochondria and nucleus maintain it at concentrations below 2.5 nM. Further, we find that the signaling molecule nitric oxide can initiate the rapid mobilization of heme in the cytosol and nucleus from certain thiol-containing factors. We also find that the glycolytic enzyme glyceraldehyde phosphate dehydrogenase constitutes a major cellular heme buffer, and is responsible for maintaining the activity of the heme-dependent nuclear transcription factor heme activator protein (Hap1p). Altogether, we demonstrate that the heme sensors can be used to reveal fundamental aspects of heme trafficking and dynamics and can be used across multiple organisms, includingEscherichia coli, yeast, and human cell lines.


2010 ◽  
Vol 249 (3) ◽  
pp. 217-223 ◽  
Author(s):  
Michael F. Hughes ◽  
Brenda C. Edwards ◽  
Karen M. Herbin-Davis ◽  
Jesse Saunders ◽  
Miroslav Styblo ◽  
...  

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