Characterization of a 47-Kilodalton Chlorophyll-Binding Polypeptide (CP-47) Isolated from a Photosystem II Core Complex
スポンサーリンク
概要
- 論文の詳細を見る
The purified photosystem II core complex from spinach with a particle size of about 480 kDa and containing five constituent polypeptides was further resolved by octyl-β-D-glucopyranoside treatment followed by separation by high-performance liquid chromatography using a gel-permeation column. Of the four clearly separated, chlorophyll-containing fractions, one with a particle size of 170-180 kDa was composed entirely of a single, 47-kDa polypeptide. This chlorophyll a-polypeptide contains p-carotene and Pheophytin a, but no plastoquinone. The number of chlorophyll a associated with this polypeptide in situ was estimated to be 6-7 and an oligomeric structure of this polypeptide in vivo was proposed on the basis of its chlorophyll/protein ratio and the isolated particle size. The complex exhibited F-695 emission, but was photochemically inactive. The amino acid composition of the apoprotein was also determined.
- 日本植物生理学会の論文
著者
-
Katoh S
Himeji Inst. Technol. Hyogo Jpn
-
Satoh K
Okayama Univ. Okayama Jpn
-
Satoh Kimiyuki
Department of Brology, Faculty of Science, Okayama University
-
Satoh Kimiyuki
Division Of Biological Regulation And Photobiology National Institute For Basic Biology:department O
-
Satoh Kimiyuki
Natl. Inst. Basic Biol. Okazaki Japan
-
Satoh Kimiyuki
Department Of Biology Faculty Of Science Okayama University
-
Satoh K
Himeji Inst. Technol. Hyogo Jpn
-
Tang Xiao-song
Department Of Biology Faculty Of Science Okayama University
関連論文
- Quantitative Determination of Changes in the Number and Size of Chloroplasts in Naturally Senescing Leaves of Rice Seedlings
- Changes in Protein Content and in the Structure and Number of Chloroplasts during Leaf Senescence in Rice Seedlings
- Relationship between Photosynthesis and Chlorophyll Content during Leaf Senescence of Rice Seedlings
- Isolation and Characterization of a Photosystem II Core Complex Depleted in the 43 kDa-Chlorophyll-Binding Subunit
- Dibromothymoquinone (DBMIB) Replaces the Function of Q_A at 77 K in the Isolated Photosystem II Reaction Center (D1-D2-Cytochrome b_) CompleX: Difference Spectrum of the P680^+(DBMIB^-) State
- SELECTIVE EXTRACTION OF β-CAROTEN FROM THE PS II REACTION CENTER AND ITS ROLE
- The Herbicide-Resistant Species of the Cyanobacterial D1 Protein Obtained by Thorough and Random in vitro Mutagenesis
- An Oxygen-Evolving Photosystem II Complex Associated with the Core Substructure of the Phycobilisome from Synechococcus elongatus
- Immunological Cross-Reactivity among Corresponding Proteins of Photosystems I and II from Widely Divergent Photosynthetic Organisms
- THE ISOLATION AND CHARACTERIZATION OFPHOTOSYSTEM II CORE COMPLEX FROM A CYANOBACTERIUM MASTIGOCLADUSLAMINOSUS
- A POWERFUL STRATEGY WITH IN VITRO RANDOM MUTAGENESIS OF GENES AND SUBSEQUENT SELECTION OF THEIR TRANSFORMANTS : ITS APPLICATION TO CONFERRING PHOTO-TOLERANCE ON D1 PROTEIN
- STRUCTURAL CHANGES OF D1 PROTEIN INPHOTO-TOLERANT CYANOBACTERIAL MUTANTS RESULTING FROM IN VITRORANDOM MUTAGENESIS OF PSBA
- PHOTO-TOLERANT MUTANTS OF SYNECHOCYSTISOBTAINED BY IN VITRO RANDOM MUTAGENESIS OF PSBA
- A Versatile Chromatographic Procedure for Purifying PS II Reaction Center Complex from Digitonin Extracts of Spinach Thylakoids
- Possible Involvement of a Low Redox Potential Component(s) Downstream of Photosystem I in the Translational Regulation of the D1 Subunit of the Photosystem II Reaction Center in Isolated Pea Chloroplasts
- AN IN VITRO ANALYSIS OF THE LIGHTREGULATED SYNTHESIS OF D1 PROTEIN IN PEA CHLOROPASTS.
- Evidence from Crosslinking for a Close Association of the Extrinsic 33 kDa Protein with the 9.4 kDa Subunit of Cytochrome b 559 and the 4.8 kDa Product of the psb I Gene in Oxygen-Evolving Photosystem II Complexes from Spinach
- Artificial Quinones Replace the Function of Quinone Electron Acceptor (Q_A) in the Isolated D1-D2-Cytochrolne b_ Photosystem II Reaction Center Complex
- Evidence from Crosslinking for Nearest-Neighbor Relationships among the Three Extrinsic Proteins of Spinach Photosystem II Complexes that are Associated with Oxygen Evolution
- Characterization of a 47-Kilodalton Chlorophyll-Binding Polypeptide (CP-47) Isolated from a Photosystem II Core Complex
- The Level of Stromal ATP Regulates Translation of the D1 Protein in Isolated Chloroplasts
- Viability of Chlamydomonas Mutants with Amino Acid Substitutions in the Precursor D1 Protein at the Carboxyl-Terminal Processing Site : an Analysis by Mixed-Culture Growth Experiments
- Mechanism of photoinactivation in photosynthetic systems IV. Light-induced changes in the fluorescence transient
- Identification of the Carboxyl-Terminal Processing Protease for the D1 Precursor Protein of the Photosystem II Reaction Center of Spinach : PROTEINS, ENZYMES AND METABOLISM : MEMBRANES AND BIOENERGETICS
- Mechanism of photoinactivation in photosynthetic systems III. Site and mode of photoinactivation in photosystem I
- Properties of light-harvesting chlorophyll a/b-protein, and photosystem I chlorophyll a-protein, purified from digitonin extracts of spinach chloroplasts by isoelectrofocusing
- Mechanism of photoinactivation in photosynthetic systems I. The dark reaction in photoinactivation
- Chromatographic Purification and Determination of the Carboxy-Terminal Sequences of Photosystem ll Reaction Center Proteins, D1 and D2
- PHOTOSYNTHETIC NITRITE REDUCTASE II. FURTHER PURIFICATION AND BIOCHEMICAL PROPERTIES OF THE ENZYME
- Mechanism of photoinactivation in photosynthetic systems II. The occurrence and properties of two different types of photoinactivation
- Effects of urea and o-phenanthroline on F-695 emission in chloroplasts
- Genetic Engineering of the Processing Site of D1 Precursor Protein of Photosystem II Reaction Center in Chlamydomenas reinhardtii