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

Eur J Biochem. 1996 Nov 15;242(1):163-70. doi: 10.1111/j.1432-1033.1996.0163r.x.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Alcohol Oxidoreductases / metabolism*
  • Chlorophyll / analogs & derivatives
  • Chlorophyll / metabolism
  • Chlorophyll A
  • Chlorophyllides / metabolism*
  • Chromatography, High Pressure Liquid
  • Hordeum
  • NADP / metabolism
  • Substrate Specificity


  • Chlorophyllides
  • Chlorophyll
  • chlorophyllide b
  • pheophorbide b
  • NADP
  • Adenosine Triphosphate
  • Alcohol Oxidoreductases
  • chlorophyll b reductase
  • Chlorophyll A