PMID: 8954166Nov 15, 1996Paper

Substrate specificity of chlorophyll(ide) b reductase in etioplasts of barley (Hordeum vulgare L.)

European Journal of Biochemistry
V ScheumannW Rüdiger

Abstract

Enzyme activity of chlorophyll(ide) b reductase is present in etioplasts. Recently the conversion of chlorophyllide b to chlorophyll a via 7(1)-hydroxychlorophyll a was demonstrated in barley etioplasts. We used zinc pheophorbide b for a detailed investigation of the reduction of the 7-formyl group to the 7(1)-hydroxy compound in intact barley etioplasts. The reaction proceeded likewise before esterification and after esterification with phytyl diphosphate. The metal-free pheophorbide b, that is not accepted by chlorophyll synthase for esterification, is reduced to 7(1)-hydroxypheophorbide a to a small extent. The zinc (13(2)S)-pheophorbide b is at least equally well accepted for reduction as the epimer with the 13(2)R configuration of natural chlorophyll b. The reaction requires NADPH or NADH, although the latter is less effective. ATP is not required for the first step to the 7(1)-hydroxy compound. The significance of chlorophyll b reduction for acclimation from shade to sun leaves and for chlorophyll degradation is discussed.

References

Dec 1, 1992·Biochemistry·M A Schneegurt, S I Beale
Oct 1, 1993·Archives of Biochemistry and Biophysics·H ItoA Tanaka
Jan 15, 1994·European Journal of Biochemistry·M HelfrichW Rüdiger
Jan 19, 1996·The Journal of Biological Chemistry·H ItoA Tanaka

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Citations

Mar 12, 2004·Annual Review of Plant Physiology and Plant Molecular Biology·Philippe MatileHoward Thomas
Sep 29, 2018·International Journal of Molecular Sciences·Weiwei LinZhaowei Li
Mar 27, 1999·FEBS Letters·V ScheumannW Rüdiger
Jul 6, 2012·The Plant Journal : for Cell and Molecular Biology·Yousuke ShimodaAyumi Tanaka
Jul 27, 1999·The Journal of Biological Chemistry·P Folly, N Engel
Dec 18, 1998·The Journal of Biological Chemistry·V ScheumannW Rüdiger

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