TY - JOUR
T1 - Use of XAS for the elucidation of metal structure and function
T2 - Applications to nickel biochemistry, molecular toxicology, and carcinogenesis
AU - Carrington, Paul E.
AU - Al-Mjeni, Faizah
AU - Zoroddu, Maria A.
AU - Costa, Max
AU - Maroney, Michael J.
PY - 2002/10
Y1 - 2002/10
N2 - Nickel has been shown to be an essential trace element involved in the metabolism of several species of bacteria, archea, and plants. In these organisms, nickel is involved in enzymes that catalyze both non-redox (e.g., urease, glyoxalase I) and redox (e.g., hydrogenase, carbon monoxide dehydrogenase, superoxide dismutase) reactions, and proteins involved in the transprt, strage, metallocenter assembly, and regulation of nickel concentration have evolved. Studies of structure/function relationship in nickel biochemistry reveal that cysteine ligands are used to stabilize the Ni(III/II) redox couple. Certain nickel compounds have also been shown to be potent human carcinogens. A likely target for carcinogenic nickel -is nuclear histone proteins. Here we present X-ray absorption spectroscopic studies of a model Ni peptide designed to help characterize the structure of the nickel complexes formed with histones and place them in the context of nickel structure/function relationships, to gain insights into the molecular mechanism of nickel carcinogenesis.
AB - Nickel has been shown to be an essential trace element involved in the metabolism of several species of bacteria, archea, and plants. In these organisms, nickel is involved in enzymes that catalyze both non-redox (e.g., urease, glyoxalase I) and redox (e.g., hydrogenase, carbon monoxide dehydrogenase, superoxide dismutase) reactions, and proteins involved in the transprt, strage, metallocenter assembly, and regulation of nickel concentration have evolved. Studies of structure/function relationship in nickel biochemistry reveal that cysteine ligands are used to stabilize the Ni(III/II) redox couple. Certain nickel compounds have also been shown to be potent human carcinogens. A likely target for carcinogenic nickel -is nuclear histone proteins. Here we present X-ray absorption spectroscopic studies of a model Ni peptide designed to help characterize the structure of the nickel complexes formed with histones and place them in the context of nickel structure/function relationships, to gain insights into the molecular mechanism of nickel carcinogenesis.
KW - Carcinogenesis
KW - Enzyme
KW - Histone
KW - Nickel
KW - Nucleosome
KW - Protein
KW - XAS
UR - http://www.scopus.com/inward/record.url?scp=0036804634&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036804634&partnerID=8YFLogxK
U2 - 10.1289/ehp.02110s5705
DO - 10.1289/ehp.02110s5705
M3 - Article
C2 - 12426116
AN - SCOPUS:0036804634
SN - 0091-6765
VL - 110
SP - 705
EP - 708
JO - Environmental Health Perspectives
JF - Environmental Health Perspectives
IS - SUPPL. 5
ER -