Catalytic function of a novel protein protochlorophyllide oxidoreductase C of Arabidopsis thaliana.
In Arabidopsis thaliana Por C has been identified only on sequence homology to that of por A and por B. To demonstrate its catalytic function Arabidopsis thaliana protochlorophyllide oxidoreductase C gene (por c) that codes for the mature part of POR C protein having 335 amino acids was expressed in Escherchia coli cells. The POR C enzyme in the presence of NADPH and protochlorophyllide when incubated in dark formed a ternary complex. When it was excited at 433 nm, it had a fluorescence emission peak at 636 nm. After illumination with actinic cool white fluorescent light, a peak at 673 nm due to chlorophyllide gradually increased with concomitant decrease of 636 nm emission, demonstrating the gradual phototransformation of protochlorophyllide to chlorophyllide. The significance of differential por gene expression in light and dark among different species is discussed.
Pattanayak
Gopal K
GK
School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
Tripathy
Baishnab C
BC
D017360:Arabidopsis / Q000201:enzymology*; D002384:Catalysis; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D005453:Fluorescence; D015151:Immunoblotting; D010088:Oxidoreductases / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011521:Protochlorophyllide / Q000378:metabolism
D011521:Protochlorophyllide; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C023886:protochlorophyllide reductase