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Excitation energy transfer study of the spatial relationship between the carbonyl and metal cofactors in pig plasma amine oxidase.

Abstract：

:9-Hydrazinoacridine irreversibly labeled pig plasma amine oxidase by covalent attachment to the active carbonyl cofactor. The visible absorption spectrum of the modified protein displays new absorption bands at 495 and 525 nm. Its emission spectrum exhibited maxima at 415 and 440 nm. In addition, both absorption and emission spectra were insensitive to pH changes between 6 and 10. Phase modulation fluorometry was used to determine fluorescence lifetimes of Zn2+- and Co2+-substituted acridinyl plasma amine oxidase. Energy transfer efficiency was 22%; the distance separating the Co2+ ion (in the copper binding site) and the acridine moiety (the amine substrate binding site) ranges between 11.7 and 14.7 A. This work defines the proximity of the metal and substrate (and hence the carbonyl cofactor) and precludes any direct interaction between Cu2+ and pyrroloquinoline quinone or between Cu2+ and the substrate.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Lamkin MS,Williams TJ,Falk MC

doi

10.1016/0003-9861(88)90105-1

subject

Has Abstract

pub_date

1988-02-15 00:00:00

pages

72-9

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90105-1

journal_volume

261

pub_type

杂志文章

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