Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity

Rozga, M; Sokolowska, M; Protas, AM; Bal, W

HERO ID

1848672

Reference Type

Journal Article

Year

2007

Language

English

PMID

17516096

HERO ID 1848672
In Press No
Year 2007
Title Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity
Authors Rozga, M; Sokolowska, M; Protas, AM; Bal, W
Journal Journal of Biological Inorganic Chemistry
Volume 12
Issue 6
Page Numbers 913-918
Abstract The conditional stability constant at pH 7.4 for Cu(II) binding at the N-terminal site (NTS) of human serum albumin (HSA) was determined directly by competitive UV-vis spectroscopy titrations using nitrilotriacetic acid (NTA) as the competitor in 100 mM NaCl and 100 mM N-(2-hydroxyethyl)piperazine-N'-ethanesulfonic acid (Hepes). The log Kc (NTS) value of 12.0 +/- 0.1 was determined for HSA dissolved in 100 mM NaCl. A false log log Kc (NTS) (c) value of 11.4 +/- 0.1 was obtained in the 100 mM Hepes buffer, owing to the formation of a ternary Cu(NTA)(Hepes) complex. The impact of the picomolar affinity of HSA for Cu(II) on the availability of these ions in neurodegenerative disorders is briefly discussed.
Doi 10.1007/s00775-007-0244-8
Pmid 17516096
Wosid WOS:000248414100018
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English
Keyword human serum albumin; copper(II); conditional stability constant