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Article

Amino acid deletions in loop C of the chlorophyll a-binding protein CP47 alter the chloride requirement and/or prevent the assembly of photosystem II.

Plant molecular biology - 1 Nov 2000

Clarke S M, Eaton-Rye J J

Abstract excerpt

The chlorophyll a-binding protein CP47 directs excitation energy to the reaction center of photosystem II (PSII) during oxygenic photosynthesis and has additional structural and functional roles associated with the PSII water-oxidizing complex. Oligonucleotide-directed mutagenesis was employed to study loop C of CP47 (approximately Trp-162 to Gly-197) which faces the thylakoid lumen. Five short amino acid...

Topics

Amino Acid Sequence
Bacterial Proteins
Chlorides
Cyanobacteria
Cytochrome c Group
Light-Harvesting Protein Complexes
Molecular Sequence Data
Mutation
Oxygen
Photosynthetic Reaction Center Complex Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Photosystem II Protein Complex

Sequence Deletion

Sequence Homology, Amino Acid

Source

Identifiers

PMID: 11198421
DOI: 10.1023/a:1026528813583

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Amino acid deletions in loop C of the chlorophyll a-binding protein CP47 alter the chloride requirement and/or prevent the assembly of photosystem II.PMID 11198421Read ↗

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Site-directed mutagenesis of the CP 47 protein of photosystem II: alteration of conserved charged residues which lie within lethal deletions of the large extrinsic loop E.Semantic proximity Read ↗

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Introduction of the 305Arg-->305Ser mutation in the large extrinsic loop E of the CP43 protein of Synechocystis sp. PCC 6803 leads to the loss of cytochrome c(550) binding to Photosystem II.Semantic proximity Read ↗

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