Characterisation of the assembly pathway of the pea NADPH:protochlorophyllide (Pchlide) oxidoreductase (POR), with emphasis on the role of its substrate, Pchlide

Physiologia Plantarum

Volumn 111, Issue 2, 2001, Pages 239-244

  Aronsson, H ^a   Sundqvist, C ^a   Timko, M P ^b   Dahlin, C ^a,c  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

^b UNIVERSITY OF VIRGINIA   (United States)

^c HALMSTAD UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; AMINOLEVULINIC ACID; BIOCHEMICAL PATHWAY; CHLOROPLAST; ENVELOPE PROTEIN; ENZYME ACTIVITY; ENZYME SUBUNIT; IN VITRO CULTURE; NADPH:PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; PEA; PROTEIN BINDING; RIBULOSEBISPHOSPHATE CARBOXYLASE; WILD RELATIVE;

EID: 0034772456     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.2001.1110216.x     Document Type: Article

References (23)

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19. Evolution of chlorophyll biosynthesis - The challenge to survive photooxidation
20. The regular ultrastructure of isolated prolamellar bodies depends on the presence of membrane-bound NADPH-protochlorophyllide oxidoreductase
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22. With chlorophyll pigments from prolamellar bodies to light-harvesting complexes
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