Role of acidic amino acid residues of PsaD subunit on limiting the affinity of photosystem I for ferredoxin

Biochemical and Biophysical Research Communications

Volumn 287, Issue 4, 2001, Pages 833-836

  Bottin, Hervé ^a   Hanley, Jonathan ^a   Lagoutte, Bernard ^a  

^a CEA SACLAY   (France)

Author keywords

Cyanobacterium; Electron transfer; Ferredoxin; Photosystem I; PsaD subunit; Synechocystis sp. PCC 6803

Indexed keywords

AMINO ACID; ARGININE; FERREDOXIN; HISTIDINE; PROTEIN PSAD; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; CYANOBACTERIUM; DISSOCIATION CONSTANT; ELECTRON; ELECTRON TRANSPORT; NONHUMAN; PHOTOSYSTEM I; PRIORITY JOURNAL; PROTEIN INTERACTION;

SYNECHOCYSTIS; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

EID: 0035812833     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.5658     Document Type: Article

References (23)

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6. The PsaC subunit of photosystem I provides an essential lysine residue for fast electron transfer to ferredoxin
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8. Ferredoxin cross-links to a 22 kDa subunit of photosystem I
9. Identification of the amino acids involved in the functional interaction between photosystem I and ferredoxin from Synechocystis sp. PCC 6803 by chemical cross-linking
10. Mutational analysis of photosystem I polypeptides: Role of PsaD and the lysyl 106 in the reductase activity of photosystem I
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20. Near infra-red absorption spectra of the chlorophyll a cations and triplet state in vitro and in vivo
21. B is the cluster interacting with soluble ferredoxin
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