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...

Full description

Bibliographic Details
Main Authors: Bauer, Nicole, Panak, Petra J.
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