Paramagnetic NMR investigations of Co(II) and Ni(II) amicyanin

被引:35
作者
Salgado, J
Kalverda, AP
Diederix, REM
Canters, GW
Moratal, JM
Lawler, AT
Dennison, C
机构
[1] Leiden Univ, Leiden Inst Chem, Gorlaeus Labs, NL-2300 RA Leiden, Netherlands
[2] Univ Valencia, Dept Quim Inorgan, E-46100 Burjassot, Valencia, Spain
[3] Natl Univ Ireland Univ Coll Dublin, Dept Chem, Dublin 4, Ireland
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 1999年 / 4卷 / 04期
关键词
amicyanin; paramagnetic NMR; metal substitution; azurin; electron transfer;
D O I
10.1007/s007750050332
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The paramagnetic H-1 NMR spectra of the Co(II) and Ni(II) substituted forms of the type 1 blue copper protein (cupredoxin) amicyanin have been assigned. This is the first such analysis of a cupredoxin, which has a distorted tetrahedral active site with the ligands provided by two histidines, a cysteine and a methionine. The isotropic shifts of the resonances in these spectra are compared with those of Co(II) and Ni(II) azurin. A number of interesting similarities and differences are found. The coordination of the metal by the two equatorial histidine ligands is very similar in both proteins. The interaction between the introduced metal and the thiolate sulfur of the equatorial cysteine ligand is enhanced in the amicyanin derivatives. Resonances belonging to the weak axial methionine ligand exhibit much larger shifts in the amicyanin derivatives, indicative of shorter M(II)-S(Met) distances. The presence of shorter axial M(II)-S(Met) and equatorial M(II)-S(Cys) distances in both Co(II) and Ni(II) amicyanin is ascribed to the absence of a second axially interacting amino acid at the active site of this cupredoxin.
引用
收藏
页码:457 / 467
页数:11
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