4.5 Article

Heme-independent soluble and membrane-associated peroxidase activity of a Zea mays annexin preparation

Journal

PLANT SIGNALING & BEHAVIOR
Volume 4, Issue 5, Pages 428-430

Publisher

TAYLOR & FRANCIS INC
DOI: 10.4161/psb.4.5.8297

Keywords

annexin; calcium; C2; lipoxygenase; maize; peroxidase

Funding

  1. BBSRC
  2. Isaac Newton Trust
  3. Cambridge Thai Foundation
  4. Brooks Fund (University of Cambridge)

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Annexins are cytosolic proteins capable of reversible, Ca2+ dependent membrane binding or insertion. Animal annexins form and regulate Ca2+-permeable ion channels and may therefore participate in signaling. Zea mays (maize) annexins (ZmANN33 and ZmANN35) have recently been shown to form a Ca2+-permeable conductance in planar lipid bilayers and also exhibit in vitro peroxidase activity. Peroxidases form a superfamily of intra- or extracellular heme-containing enzymes that use H2O2 as the electron acceptor in a number of oxidative reactions. Maize annexin peroxidase activity appears independent of heme and persists after membrane association, the latter suggesting a role in reactive oxygen species signaling.

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