Ternary ligand-zinc-hydroxamate complexes

Yu Hung Chiu, Gregory J. Gabriel, James Canary

Research output: Contribution to journalArticle

Abstract

Because of the importance of the hydroxamic acid functional group in zinc protease inhibitors, we have measured the stability constants of the ternary complex LMG, where L is series of tridentate and tetradentate ligands containing amino, carboxylate, pyridyl, and/or imidazolyl groups as enzyme models and G is the guest molecule, acetohydroxamate or N-methylacetohydroxamate. All measurements were determined by pH titration which gave reproducible and reasonable results. A general correlation between binding of LMG and that of LM showed ligands that strongly chelated zinc gave less LMG formation. Surprisingly, no correlation was observed between ligand charge and LMG formation even though the guest, acetohydroxamate, is anionic. The pH value of the maximum formation of the ternary complex is also correlated to the acidity of zinc-bound water; more acidic zinc-bound water results in a maximum ternary complex formation at lower pH value.

Original languageEnglish (US)
Pages (from-to)40-44
Number of pages5
JournalInorganic Chemistry
Volume44
Issue number1
DOIs
StatePublished - Jan 10 2005

Fingerprint

Zinc
zinc
Ligands
ligands
Hydroxamic Acids
protease
Water
Protease Inhibitors
Titration
Acidity
acidity
titration
inhibitors
Functional groups
water
carboxylates
enzymes
acids
Molecules
Enzymes

ASJC Scopus subject areas

  • Inorganic Chemistry

Cite this

Ternary ligand-zinc-hydroxamate complexes. / Chiu, Yu Hung; Gabriel, Gregory J.; Canary, James.

In: Inorganic Chemistry, Vol. 44, No. 1, 10.01.2005, p. 40-44.

Research output: Contribution to journalArticle

Chiu, Yu Hung ; Gabriel, Gregory J. ; Canary, James. / Ternary ligand-zinc-hydroxamate complexes. In: Inorganic Chemistry. 2005 ; Vol. 44, No. 1. pp. 40-44.
@article{8d476ffbb5d04113a68a7bce6fdf6e57,
title = "Ternary ligand-zinc-hydroxamate complexes",
abstract = "Because of the importance of the hydroxamic acid functional group in zinc protease inhibitors, we have measured the stability constants of the ternary complex LMG, where L is series of tridentate and tetradentate ligands containing amino, carboxylate, pyridyl, and/or imidazolyl groups as enzyme models and G is the guest molecule, acetohydroxamate or N-methylacetohydroxamate. All measurements were determined by pH titration which gave reproducible and reasonable results. A general correlation between binding of LMG and that of LM showed ligands that strongly chelated zinc gave less LMG formation. Surprisingly, no correlation was observed between ligand charge and LMG formation even though the guest, acetohydroxamate, is anionic. The pH value of the maximum formation of the ternary complex is also correlated to the acidity of zinc-bound water; more acidic zinc-bound water results in a maximum ternary complex formation at lower pH value.",
author = "Chiu, {Yu Hung} and Gabriel, {Gregory J.} and James Canary",
year = "2005",
month = "1",
day = "10",
doi = "10.1021/ic0493090",
language = "English (US)",
volume = "44",
pages = "40--44",
journal = "Inorganic Chemistry",
issn = "0020-1669",
publisher = "American Chemical Society",
number = "1",

}

TY - JOUR

T1 - Ternary ligand-zinc-hydroxamate complexes

AU - Chiu, Yu Hung

AU - Gabriel, Gregory J.

AU - Canary, James

PY - 2005/1/10

Y1 - 2005/1/10

N2 - Because of the importance of the hydroxamic acid functional group in zinc protease inhibitors, we have measured the stability constants of the ternary complex LMG, where L is series of tridentate and tetradentate ligands containing amino, carboxylate, pyridyl, and/or imidazolyl groups as enzyme models and G is the guest molecule, acetohydroxamate or N-methylacetohydroxamate. All measurements were determined by pH titration which gave reproducible and reasonable results. A general correlation between binding of LMG and that of LM showed ligands that strongly chelated zinc gave less LMG formation. Surprisingly, no correlation was observed between ligand charge and LMG formation even though the guest, acetohydroxamate, is anionic. The pH value of the maximum formation of the ternary complex is also correlated to the acidity of zinc-bound water; more acidic zinc-bound water results in a maximum ternary complex formation at lower pH value.

AB - Because of the importance of the hydroxamic acid functional group in zinc protease inhibitors, we have measured the stability constants of the ternary complex LMG, where L is series of tridentate and tetradentate ligands containing amino, carboxylate, pyridyl, and/or imidazolyl groups as enzyme models and G is the guest molecule, acetohydroxamate or N-methylacetohydroxamate. All measurements were determined by pH titration which gave reproducible and reasonable results. A general correlation between binding of LMG and that of LM showed ligands that strongly chelated zinc gave less LMG formation. Surprisingly, no correlation was observed between ligand charge and LMG formation even though the guest, acetohydroxamate, is anionic. The pH value of the maximum formation of the ternary complex is also correlated to the acidity of zinc-bound water; more acidic zinc-bound water results in a maximum ternary complex formation at lower pH value.

UR - http://www.scopus.com/inward/record.url?scp=11244352094&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=11244352094&partnerID=8YFLogxK

U2 - 10.1021/ic0493090

DO - 10.1021/ic0493090

M3 - Article

C2 - 15627358

AN - SCOPUS:11244352094

VL - 44

SP - 40

EP - 44

JO - Inorganic Chemistry

JF - Inorganic Chemistry

SN - 0020-1669

IS - 1

ER -