NDLI: Concentration and function of membrane-bound cytochromes in cyanobacterial heterocysts.

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Concentration and function of membrane-bound cytochromes in cyanobacterial heterocysts.

Content Provider	Semantic Scholar
Author	Houchins, J. P. Hind, Geoffrey
Copyright Year	1984
Abstract	Membranes isolated from heterocysts and vegetative cells of Anabaena 7120 were assayed for content of cytochrome f, cytochrome b-563, cytochrome b-559(HP), cytochrome b-559(LP), and cytochrome aa(3) by use of reduced-minus-oxidized difference spectra. The level of cytochrome aa(3) 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-559(HP) but contain cytochrome b-559(LP) (E(m7.5) = +77 millivolts, n = 1) at approximately the same concentration as cytochrome f. The role of cytochrome b-559(LP) 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-559(LP) indicating that this cytochrome is not directly involved in this pathway.
Starting Page	51
Ending Page	54
Page Count	4
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.plantphysiol.org/content/plantphysiol/76/2/456.full.pdf
PubMed reference number	16663864v1
Volume Number	76
Issue Number	2
Journal	Plant physiology
Language	English
Access Restriction	Open
Subject Keyword	Anabaena Cyanobacteria Cyanophage PSS2 Cytochromes Electron Transport Hydrogenase Plastoquinone Tissue membrane cytochrome activity
Content Type	Text
Resource Type	Article

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