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. 1984 Oct;76(2):456–460. doi: 10.1104/pp.76.2.456

Concentration and Function of Membrane-Bound Cytochromes in Cyanobacterial Heterocysts 1

Jeffrey P Houchins 1,2, Geoffrey Hind 1
PMCID: PMC1064310  PMID: 16663864

Abstract

Membranes isolated from heterocysts and vegetative cells of Anabaena 7120 were assayed for content of cytochrome f, cytochrome b-563, cytochrome b-559HP, cytochrome b-559LP, and cytochrome aa3 by use of reduced-minus-oxidized difference spectra. The level of cytochrome aa3 in heterocyst membranes was 4 to 100 times higher than that in vegetative cells of Anabaena 7120 or other species of cyanobacteria. Heterocyst membranes lack cytochrome b-559HP but contain cytochrome b-559LP (Em7.5 = +77 millivolts, n = 1) at approximately the same concentration as cytochrome f. The role of cytochrome b-559LP in the hydrogenase-dependent electron transfer pathway was investigated with the inhibitor 2-(n-heptyl)-4-hydroxyquinoline N-oxide which blocks electron flow from hydrogenase to acceptors reacting with the plastoquinone pool. Addition of inhibitor elicited no change in the reduction level of cytochrome b-559LP indicating that this cytochrome is not directly involved in this pathway.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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