Two Protochlorophyllide Reductases to Make Chlorophyll Green: Structural and Evolutionary Aspects

• FUJITA Yuichi

  Graduate School of Bioagricultural Sciences, Nagoya University / PRESTO, JST

• KURISU Genji

  Institute for Protein Research, Osaka University

Bibliographic Information

Other Title

• クロロフィルを緑にする２つの還元酵素：　光依存型酵素と暗所作動型酵素の反応機構と進化的考察
• クロロフィル オ ミドリ ニ スル フタツ ノ カンゲン コウソ ヒカリ イソンガタ コウソ ト アンショサドウガタ コウソ ノ ハンノウ キコウ ト シンカテキ コウサツ

Abstract

Protochlorophyllide (Pchlide) reduction is the final step to make up the spectroscopic properties of chlorophyll a in biosynthesis of chlorophyll. During evolution, photosynthetic organisms have invented two structurally unrelated Pchlide reductases; light-dependent Pchlide reductase (LPOR) and light-independent (dark-operative) Pchlide reductase (DPOR). LPOR is an NADPH-dependent enzyme operating as a key enzyme for the light-dependent greening in angiosperms, and DPOR is a nitrogenase-like enzyme that allows gymnosperms, algae, cyanobacteria and photosynthetic bacteria to produce (bacterio)chlorophylls even in the dark. We will review recent major research progresses on Pchlide reductases, especially, crystallographic structure and proposed reaction mechanism of DPOR. Differential operation and evolutionary implications of these enzymes are also discussed.<br>

Journal

• Seibutsu Butsuri

  Seibutsu Butsuri 51 (2), 066-071, 2011

  The Biophysical Society of Japan General Incorporated Association

Keywords

• protochlorophyllide
• dark-operative protochlorophyllide reductase
• nitrogenase
• chlorophyll biosynthesis

Details

• CRID: 1390001206534176384
• NII Article ID: 10028105757
• NII Book ID: AN00129693
• DOI: 10.2142/biophys.51.066
• ISSN: 13474219
• ISSN: 05824052
• NDL BIB ID: 11057500
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I11057500
• Web Site: http://www.jstage.jst.go.jp/article/biophys/51/2/51_2_066/_pdf
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed