1H NMR and NOE studies of the purple acid phosphatases from porcine uterus and bovine spleen.

Abstract:

:The diiron active sites of the purple acid phosphatases from porcine uterus (also called uteroferrin, Uf) and bovine spleen (BSPAP) and their complexes with tungstate are compared by 1H NMR and NOE techniques. The paramagnetically shifted features of the 1H NMR spectrum of reduced BSPAP are similar to those of reduced Uf, while the spectra of the tungstate complexes are almost identical. These observations suggest that the two active sites are quite similar, in agreement with the greater than 90% sequence homology found in the two enzymes. Nuclear Overhauser effect (NOE) experiments on the His N-H resonances show that the Fe(III)-His residue is N epsilon-coordinated, while the Fe(II)-His is H delta-coordinated in both enzymes. On the basis of the above NMR and NOE results, our previously proposed model for the dinuclear iron active site of Uf [Scarrow, R. C., Pyrz, J. W., & Que, L., Jr. (1990) J. Am. Chem. Soc. 112, 657-665] is corroborated, refined, and found to represent the diiron center of BSPAP as well.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Wang Z,Ming LJ,Que L Jr,Vincent JB,Crowder MW,Averill BA

doi

10.1021/bi00138a004

subject

Has Abstract

pub_date

1992-06-16 00:00:00

pages

5263-8

issue

23

eissn

0006-2960

issn

1520-4995

journal_volume

31

pub_type

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