Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS)
The complexation of Cm(III) with transferrin is investigated in the pH range from 3.5 to 11.0 in the absence of carbonate and at c(carbonate)tot = 25 mM. In the absence of carbonate two Cm(III) transferrin species I and II are formed depending on pH. An increase of the total carbonate concentration...
Main Authors: | , |
---|---|
Format: | Text |
Language: | English |
Published: |
Karlsruhe
2015
|
Subjects: | |
Online Access: | https://dx.doi.org/10.5445/ir/1000046565 https://publikationen.bibliothek.kit.edu/1000046565 |
id |
ftdatacite:10.5445/ir/1000046565 |
---|---|
record_format |
openpolar |
spelling |
ftdatacite:10.5445/ir/1000046565 2023-05-15T15:52:44+02:00 Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS) Bauer, Nicole Panak, Petra J. 2015 PDF https://dx.doi.org/10.5445/ir/1000046565 https://publikationen.bibliothek.kit.edu/1000046565 en eng Karlsruhe KITopen License Open Access info:eu-repo/semantics/openAccess https://publikationen.bibliothek.kit.edu/kitopen-lizenz carbonic acid curium ferric ion transferrin Text article-journal Journal Article ScholarlyArticle 2015 ftdatacite https://doi.org/10.5445/ir/1000046565 2021-11-05T12:55:41Z The complexation of Cm(III) with transferrin is investigated in the pH range from 3.5 to 11.0 in the absence of carbonate and at c(carbonate)tot = 25 mM. In the absence of carbonate two Cm(III) transferrin species I and II are formed depending on pH. An increase of the total carbonate concentration favors the formation of the Cm(III) transferrin species II with Cm(III) bound at the Fe(III) binding site of transferrin at significantly lower pH values. The spectroscopic results directly prove that carbonate acts as a synergistic anion for Cm(III) complexation at the binding site of transferrin. At c(carbonate)tot = 25 mM the formation of the nonspecific Cm(III) transferrin species I is suppressed completely. Instead, three Cm(III) carbonate species Cm(CO3)+, Cm(CO3)2- and Cm(CO3)33- are formed successively with increasing pH. The formation of Cm(III) carbonate species results in a decreased fraction of the Cm(III) transferrin species II at pH [greater-than-or-equal] 7.4 which indicates that carbonate complexation is an important competition reaction for Cm(III) transferrin complexation at physiological carbonate concentration. Text Carbonic acid DataCite Metadata Store (German National Library of Science and Technology) |
institution |
Open Polar |
collection |
DataCite Metadata Store (German National Library of Science and Technology) |
op_collection_id |
ftdatacite |
language |
English |
topic |
carbonic acid curium ferric ion transferrin |
spellingShingle |
carbonic acid curium ferric ion transferrin Bauer, Nicole Panak, Petra J. Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS) |
topic_facet |
carbonic acid curium ferric ion transferrin |
description |
The complexation of Cm(III) with transferrin is investigated in the pH range from 3.5 to 11.0 in the absence of carbonate and at c(carbonate)tot = 25 mM. In the absence of carbonate two Cm(III) transferrin species I and II are formed depending on pH. An increase of the total carbonate concentration favors the formation of the Cm(III) transferrin species II with Cm(III) bound at the Fe(III) binding site of transferrin at significantly lower pH values. The spectroscopic results directly prove that carbonate acts as a synergistic anion for Cm(III) complexation at the binding site of transferrin. At c(carbonate)tot = 25 mM the formation of the nonspecific Cm(III) transferrin species I is suppressed completely. Instead, three Cm(III) carbonate species Cm(CO3)+, Cm(CO3)2- and Cm(CO3)33- are formed successively with increasing pH. The formation of Cm(III) carbonate species results in a decreased fraction of the Cm(III) transferrin species II at pH [greater-than-or-equal] 7.4 which indicates that carbonate complexation is an important competition reaction for Cm(III) transferrin complexation at physiological carbonate concentration. |
format |
Text |
author |
Bauer, Nicole Panak, Petra J. |
author_facet |
Bauer, Nicole Panak, Petra J. |
author_sort |
Bauer, Nicole |
title |
Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS) |
title_short |
Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS) |
title_full |
Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS) |
title_fullStr |
Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS) |
title_full_unstemmed |
Influence of carbonate on the complexation of Cm(III) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS) |
title_sort |
influence of carbonate on the complexation of cm(iii) with human serum transferrin studied by time-resolved laser fluorescence spectroscopy (trlfs) |
publisher |
Karlsruhe |
publishDate |
2015 |
url |
https://dx.doi.org/10.5445/ir/1000046565 https://publikationen.bibliothek.kit.edu/1000046565 |
genre |
Carbonic acid |
genre_facet |
Carbonic acid |
op_rights |
KITopen License Open Access info:eu-repo/semantics/openAccess https://publikationen.bibliothek.kit.edu/kitopen-lizenz |
op_doi |
https://doi.org/10.5445/ir/1000046565 |
_version_ |
1766387832087117824 |