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TitleAntioxidant capacities of green and cyanic leaves in the sun species, Quintinia serrata
Publication TypeJournal Article
Year of Publication2002
AuthorsNeill, S.O., Gould K.S., Kilmartin P.A., Mitchell K.A., and Markham K.R.
JournalFunctional Plant Biology
Volume29
Issue12
Pagination1437 - 1443
Date Published2002
ISSN14454408 (ISSN)
Keywordsantioxidant, Antioxidants, biosynthesis, Elatostema, leaf, Photochemical reactions, photoprotection, Plant cell culture, Plants (botany), Quintinia, Reactive oxygen species
AbstractAnthocyanins scavenge harmful reactive oxygen species (ROS), and may provide antioxidative protection within plant cells. For the shade species Elatostema rugosum A. Cunn., it was recently established that red-leaved morphs held a significant antioxidant advantage over green morphs. It is not known whether anthocyanins confer the same protection in sun species that are exposed to elevated levels of irradiation and thus greater photooxidative stress. Quintinia serrata A. Cunn., a canopy tree species, is polymorphic for anthocyanin expression. Levels of antioxidants in leaves of red and green morphs of Q. serrata were identified, and activities quantified using enzymatic and α,α-diphenyl-β-picrylhydrazyl (DPPH) assays and cyclic voltammetry. Both morphs contained similar levels of superoxide dismutase, catalase, ascorbic peroxidase and hydroxycinnamic acids, and showed similar ranges in DPPH scavenging activity and voltammetric profiles. Anthocyanin concentrations increased with leaf age in red morphs and were positively correlated with the extent of DPPH scavenging. However, hydroxycinnamic acids were the most active methanol-extractable fraction in both morphs, contributing 27% more to the overall low-molecular-weight antioxidant pool in the green morph than in the red. We conclude that anthocyanin biosynthesis can enhance, but is not a prerequisite for, oxidative protection in Q. serrata leaves. The possibility that anthocyanins provide a versatile mechanism for photoprotection is discussed.
URLhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0036944924&partnerID=40&md5=48969207e7e7b2b96805e1b961105347
DOI10.1071/FP02100

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