Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as a substrate.

Abstract:

:The Mg-dechelating activity of extracts of Chenopodium album (goosefoot) was investigated using an artificial substrate, chlorophyllin a. The activity was measured spectrophotometrically by the formation of a reaction product, pheophorbin a (Mg-free chlorin), after release of the central Mg. The Mg-releasing protein was highly purified by successive DEAE, Butyl and HW-55 chromatographies. The molecular weight of the purified protein was 20 k by gel filtration. The protein showed a broad, but single, pH optimum at 7.5. The K (m) value for chlorophyllin a was 95.1 nM at pH 7.5. The Mg-releasing protein was not active with chlorophyllide a, a native substrate, although it was active with Zn-chlorophyllin a. Similar results were obtained from horseradish peroxidase. Only a small molecular weight, metal-chelating substance (MCS) had Mg-dechelating activity for the native substrate. An inhibitor study showed involvement of radicals in the Mg-dechelation of the Mg-releasing protein. The purified Mg-releasing protein showed neither peroxidase activity nor absorption bands in the visible region, and this indicates that the Mg-releasing protein is clearly distinct from horseradish peroxidase, which is a heme-containing protein. A likely conclusion is that the Mg-releasing protein and horseradish peroxidase are not involved in the Mg-dechelation in the degradation pathway of chlorophylls. The relevance of the participation of MCS in Mg-dechelation in the breakdown of chlorophylls (Chls) is also discussed.

journal_name

Photosynth Res

journal_title

Photosynthesis research

authors

Suzuki T,Shioi Y

doi

10.1023/A:1020915812770

subject

Has Abstract

pub_date

2002-01-01 00:00:00

pages

217-23

issue

2

eissn

0166-8595

issn

1573-5079

journal_volume

74

pub_type

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