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EPR studies of spin-labeled bovine plasma amine oxidase: the nature of the substrate-binding site.

Abstract：

:The carbonyl cofactor of bovine plasma amine oxidase (EC 1.4.3.6), recently shown to be 6-hydroxydopa (also known as topa), has been spin labeled to the extent of one label per enzyme dimer molecule, using 4-amino-2,2,6,6-tetramethylpiperidine-N-oxyl (4-amino-TEMPO) and 4-hydrazino-TEMPO followed by reduction with borohydride. By studying the EPR spectra of the labeled enzyme, it has been deduced that there is no magnetic interaction between the copper and the spin label, and that the spin label is at least 1.3 nm distant from the copper(II) ion in the resting enzyme. The bound label is strongly immobilized, is in a sterically constricted environment, and is not accessible to small anions. Removal of the copper does not alter the EPR spectrum of the label. The results are similar to results for porcine plasma amine oxidase, and show that the copper is not close to, and does not directly interact with, the topa-bound substrate.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Greenaway FT,O'Gara CY,Marchena JM,Poku JW,Urtiaga JG,Zou Y

doi

10.1016/0003-9861(91)90362-m

subject

Has Abstract

pub_date

1991-03-01 00:00:00

pages

291-6

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(91)90362-M

journal_volume

285

pub_type

杂志文章

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