Conformational changes in plastocyanin.

Abstract:

:The visible and near-uv absorption and circular dichroic spectra were determined for spinach and poplar plastocyanin under a variety of conditions. The visible spectra showed that the copper center was invariant to changes in species, chemical modification with ethylenediamine, and addition of high concentrations of salt [2.7 M (NH4)2SO4]. In contrast, the near-uv spectra were sensitive to these conditions. Reduction of plastocyanin also altered its near-uv absorption and circular dichroic spectra. It is unlikely that these spectral changes were due to charge transfer bands since the near-uv CD spectrum of apo-plastocyanin was almost identical to that of reduced plastocyanin. There were no corresponding changes in the far-uv spectra which monitor protein secondary structure. The most likely explanation is that the protein has a flexible tertiary conformation. Conformational changes may be important in regulating electron transport. If plastocyanin is a mobile electron carrier, differential binding of the oxidized and reduced forms of plastocyanin to its reaction partners cytochrome f and P700 could facilitate electron transport.

journal_name

Arch Biochem Biophys

authors

Draheim JE,Anderson GP,Pan RL,Rellick LM,Duane JW,Gross EL

doi

10.1016/0003-9861(85)90259-0

subject

Has Abstract

pub_date

1985-02-15 00:00:00

pages

110-7

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(85)90259-0

journal_volume

237

pub_type

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