scholarly journals Characterization of the DNA-Mediated Oxidation of Dps, A Bacterial Ferritin

2016 ◽  
Vol 138 (35) ◽  
pp. 11290-11298 ◽  
Author(s):  
Anna R. Arnold ◽  
Andy Zhou ◽  
Jacqueline K. Barton
2012 ◽  
Vol 134 (26) ◽  
pp. 10822-10832 ◽  
Author(s):  
Alice S. Pereira ◽  
Cristina G. Timóteo ◽  
Márcia Guilherme ◽  
Filipe Folgosa ◽  
Sunil G. Naik ◽  
...  

Holzforschung ◽  
2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Yuko Ono ◽  
Miyuki Takeuchi ◽  
Yaxin Zhou ◽  
Akira Isogai

Abstract Eucalyptus (Eucalyptus globulus) cellulose was isolated from wood powder by dewaxing, delignification, and subsequent 4% NaOH extraction. 2,2,6,6-Tetramethyl-piperidine-1-oxyl (TEMPO)-oxidized eucalyptus celluloses were prepared from never-dried eucalyptus cellulose (EC) in yields of 96% and 72% (based on the dry weight of EC) when oxidized with NaOCl of 5 and 10 mmol/g-EC, respectively. Their carboxy contents were 1.4 and 1.8 mmol/g, respectively, when determined by conductivity titration. The crystallinity of cellulose I for EC decreased by TEMPO-mediated oxidation, showing that the originally crystalline region in EC was partly converted to disordered regions by TEMPO-mediated oxidation. Correspondingly, the relative signal area of C6‒OH/C1 with the trans-gauche (tg) conformation attributed to crystalline cellulose I in the solid-state 13C NMR spectrum of EC decreased from 0.42 to 0.34 by TEMPO-mediated oxidation with NaOCl of 10 mmol/g-EC. TEMPO-oxidized EC prepared with NaOCl of 10 mmol/g-EC was almost completely converted into individual TEMPO-oxidized EC nanofibrils (TEMPO-ECNFs) of homogeneous widths of ∼3 nm widths and lengths of >1 μm by mechanical disintegration in water. However, the TEMPO-ECNFs contained many kinks and had uneven surfaces, probably owing to significant damage occurring on the surface cellulose molecules of crystalline cellulose microfibrils during TEMPO-mediated oxidation.


Cellulose ◽  
2017 ◽  
Vol 24 (9) ◽  
pp. 3767-3775 ◽  
Author(s):  
Buapan Puangsin ◽  
Hiroto Soeta ◽  
Tsuguyuki Saito ◽  
Akira Isogai

2002 ◽  
Vol 30 (4) ◽  
pp. 713-715 ◽  
Author(s):  
S. Reindel ◽  
C. L. Schmidt ◽  
S. Anemüller ◽  
B. F. Matzanke

An iron-rich protein was isolated from the Archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC 7942. It consists of 20 kDa subunits, forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 103 Fe ions/mol of holoprotein. CD spectra are consistent with an α-helical contribution of 58%. The UV/visible spectrum provides no evidence for the presence of haem groups. This protein exhibits features of a non-haem-type bacterial ferritin although it shares only little sequence homology with non-haem bacterial ferritin.


Biochemistry ◽  
1995 ◽  
Vol 34 (26) ◽  
pp. 8415-8421 ◽  
Author(s):  
Emily Miao ◽  
Subhendu Joardar ◽  
Chunsong Zuo ◽  
Normand J. Cloutier ◽  
Atsushi Nagahisa ◽  
...  
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