Cytochrome cs from Rhodymenia palmata and Porphyra umbilicalis and the amino acid sequences of their N-terminal regions

Meatyard, Barry T.; Scawen, Michael D.; Ramshaw, John A. M.; Boulter, D.

doi:10.1016/0031-9422(75)85337-4

Cited by 9 publications

(1 citation statement)

References 33 publications

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“…Cytochrome c sequence data from the green alga Enteromorpha intestinalis [24] and the two red algae Rhodymenia palmatu and Porphyra umbilicalis [25] are also available. Although little can be said, due to the limitations in the amount of data available, of the relationship of the various algal groups, it is already clear that the algae are an evolutionary very diverse group.…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

Ferredoxin from a Red Alga, Porphyra umbilicalis

Andrew

Rogers

Boulter

et al. 1976

European Journal of Biochemistry

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A plant‐algal type ferredoxin was isolated from the red alga, Porphyra umbilicalis. In its oxidised form the ferredoxin had absorption maxima at 277, (281), 323, 420 and 462 nm. Two atoms each of non‐haem iron and labile sulphur were present per molecule protein. The midpoint potential of the protein was 400 mV and it effectively mediated electron transport in the NADP‐photoreduction system of barley. The amino acid composition of Porphyra umbilicalis ferredoxin was determined as (Lyso4 His2, Argi, Asx10, Thr8, Ser7 Glx16–17, Pro3, G1y7, A1a8, Cys5, Val6, Meti, Ile5, Leu8, Tyr5, Phe2). The minimum molecular weight of approximately 11000 was confirmed by sedimentationequilibrium studies in the analytical ultracentrifuge. Approaching half of the total amino acid sequence was determined by means of an automatic sequencer.

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Section: N-terminal Amino Acid Sequencementioning

confidence: 99%