메뉴 건너뛰기




Volumn 1482, Issue 1-2, 2000, Pages 84-91

Plant lipocalins: Violaxanthin de-epoxidase and zeaxanthin epoxidase

Author keywords

Carotenoid; Lipocalin; Plant; Violaxanthin de epoxidase; Xanthophyll cycle; Zeaxanthin epoxidase

Indexed keywords

CAROTENOID; ENZYME; LIPOCALIN; VIOLAXANTHIN; XANTHOPHYLL; ZEAXANTHIN;

EID: 0034684163     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00141-2     Document Type: Review
Times cited : (142)

References (55)
  • 4
    • 0030995292 scopus 로고    scopus 로고
    • Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves
    • (1997) Physiol. Plant. , vol.99 , pp. 197-209
    • Gilmore, A.M.1
  • 7
  • 9
    • 0001227304 scopus 로고
    • Lichtbedingte pH-Erniedrigung in einem Chloroplasten-Kompartiment als Ursache der enzymatischen Violaxanthin→Zeaxanthin-Umwandlung; Beziehungen zur Photophosphorylierung
    • (1969) Planta , vol.89 , pp. 224-243
    • Hager, A.1
  • 14
    • 0002368978 scopus 로고
    • Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching: evidence that antheraxanthin explains zeaxanthin-independent quenching
    • (1993) Photosynth. Res. , vol.35 , pp. 67-78
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 15
    • 0007709136 scopus 로고    scopus 로고
    • A.M. Gilmore, T.L. Hazlett, Govindjee, Xanthophyll cycle-dependent quenching of photosystem II chlorophyll a fluorescence: formation of a quenching complex with a short fluorescence lifetime, Proc. Natl. Acad. Sci. USA 92 (1995) 2273-2277.
  • 16
    • 0007638329 scopus 로고    scopus 로고
    • A.M. Gilmore, T.L. Hazlett, P.G. Debrunner, Govindjee, Photosystem II chlorophyll a fluorescence lifetimes and intensity are independent of the antenna size differences between barley wild-type and chlorina mutants: photochemical quenching and xanthophyll cycle-dependent nonphotochemical quenching of fluorescence, Photosynth. Res. 48 (1996) 171-187.
  • 19
    • 0016162088 scopus 로고
    • Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. III. Reaction kinetics and effect of light intensity on de-epoxidase activity and substrate availability
    • (1974) Biochim. Biophys. Acta , vol.357 , pp. 144-150
    • Siefermann, D.1    Yamamoto, H.Y.2
  • 24
    • 0028004703 scopus 로고
    • Localization of the xanthophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease
    • (1994) Planta , vol.192 , pp. 581-589
    • Hager, A.1    Holocher, K.2
  • 26
    • 0007595213 scopus 로고    scopus 로고
    • D.C. Rockholm, H.Y. Yamamoto, Purification of violaxanthin de-epoxidase by lipid affinity precipitation, in: H.Y. Yamamoto, C.M. Smith (Eds.), Photosynthetic Responses to the Environment, American Society of Plant Physiologists, Rockville, MD, 1993, p. 237.
  • 27
    • 0030060496 scopus 로고    scopus 로고
    • Violaxanthin de-epoxidase: purification of a 43-kilodalton lumenal protein from lettuce by lipid-affinity precipitation with monogalactosyldiacylglyceride
    • (1996) Plant Physiol. , vol.110 , pp. 697-703
    • Rockholm, D.C.1    Yamamoto, H.Y.2
  • 36
    • 0027966114 scopus 로고
    • Epoxidation of zeaxanthin and antheraxanthin reverses non-photochemical quenching of photosystem II chlorophyll a fluorescence in the presence of trans-thylakoid ΔpH
    • (1994) FEBS Lett. , vol.350 , pp. 271-274
    • Gilmore, A.M.1    Mohanty, N.2    Yamamoto, H.Y.3
  • 45
    • 0030292476 scopus 로고    scopus 로고
    • 8-barrel in the pathway of β-carotene biosynthesis: lycopene cyclase has an amino acid sequence similar to that of xylose isomerase
    • (1996) Biochem. J. , vol.319 , pp. 1005-1006
    • Janecek, S.1
  • 49
    • 0023609533 scopus 로고
    • 1-acid glycoprotein and serum retinol-binding protein and its relatives
    • (1987) FASEB J. , vol.1 , pp. 209-214
    • Pervaiz, S.1    Brew, K.2
  • 51
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 53
    • 0025117557 scopus 로고
    • Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins
    • (1990) J. Mol. Evol. , vol.30 , pp. 140-145
    • Wistow, G.1
  • 54
    • 0030725582 scopus 로고    scopus 로고
    • The crystallins: genes, proteins and diseases
    • (1997) Biol. Chem. , vol.378 , pp. 1331-1348
    • Graw, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.