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Secondary structure...
Secondary structure of NADPH : protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods
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- Birve, Simon, 1964- (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
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- Selstam, Eva, 1945- (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC),Eva Selstam
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Johansson, L B A (författare)
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(creator_code:org_t)
- 1996
- 1996
- Engelska.
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Ingår i: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 317:2, s. 549-555
- Relaterad länk:
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https://urn.kb.se/re...
Abstract
Ämnesord
Stäng
- To study the secondary structure of the enzyme NADPH:protochlorophyllide oxidoreductase (PCOR), a novel method of enzyme isolation was developed. The detergent isotridecyl poly(ethylene glycol) ether (Genapol X-080) selectively solubilizes the enzyme from a prolamellar-body fraction isolated from wheat (Triticum aestivum L.). The solubilized fraction was further purified by ion-exchange chromatography. The isolated enzyme was studied by fluorescence spectroscopy at 77 K, and by CD spectroscopy. The fluorescence-emission spectra revealed that the binding properties of the substrate and co-substrate were preserved and that photo-reduction occurred. The CD spectra of PCOR were analysed for the relative amounts of the secondary structures, alpha-helix, beta-sheet, turn and random coil. The secondary structure composition was estimated to be 33% alpha-helix, 19% beta-sheet, 20% turn and 28% random coil. These values are in agreement with those predicted by the Predict Heidelberg Deutschland and self-optimized prediction method from alignments methods. The enzyme has some amino acid identity with other NADPH-binding enzymes containing the Rossmann fold. The Rossmann-fold fingerprint motif is localized in the N-terminal region and at the expected positions in the predicted secondary structure. It is suggested that PCOR is anchored to the interfacial region of the membrane by either a beta-sheet or an alpha-helical region containing tryptophan residues. A hydrophobic loop-region could also be involved in membrane anchoring.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
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