Photosynthetically-linked oxidation of diaminobenzidine in blue-green algae

Lauritis, J. A.; Vigil, Eugene L.; Sherman, Louis A.; Swift, Hewson

doi:10.1016/s0022-5320(75)80034-7

Cited by 11 publications

(4 citation statements)

References 21 publications

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“…Marty (16) has obtained similar results with Coleus chloroplasts. Contrary to these, Lauritus et al (15) have found that the photooxidation of DAB by photosynthetic lamellae in Microcystis, Anacystis and Nostoc is sensitive to DCMU. Though there seems to exist some discrepancy among these results, clean-cut evidence has been obtained from the study of some mutant strains of Chlamydomonas defective in the PS-I or II activity by Chua (6), who has found that the former strain fails to conduct the DAB photooxidation, while the latter does not.…”

Section: Discussionmentioning

confidence: 85%

“…He also has pointed out a possibility that when the chloroplasts treated with MV are irradiated, MV is reduced to a radical by the action of the PS-I, and the radical produced, in turn, reduces oxygen to superoxide radical (5). In view of the facts that hydrogen peroxide enhances the DAB photooxidation by photosynthetic lamellae in Microcystis and others (15), and that DAB is oxidized by peroxidase in the presence of hydrogen peroxide (10), it seems necessary to check the possible role of endogenous active oxygen on the DAB photooxidation by isolated chloroplasts. Attempts to scavenge endogenous active oxygen, if any, by the addition of CATL and SOD, solitary or combined, were carried out.…”

Section: Discussionmentioning

confidence: 99%

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Cytochemical study of diaminobenzidine oxidation by isolated Vicia chloroplasts under illumination.

Imaizumi

Hiraoka

1982

Acta Histochem. Cytochem

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A concurrent microchemical and topochemical study of DAB* oxidation by isolated chloroplasts of Vicia faba under illumination was carried out. A new method for the quantification of the oxidation product of DAB was explored.The microchemical analysis by this method revealed that the photosystem responsible for the DAB oxidation was the PS-I. It also proved that endogenous active oxygen in the chloroplasts played only a little role in the oxidation.The topochemical analysis revealed that both the grana and the stroma membrane were positive in DAB photooxidation. The densitometric traces across the grana membranes in both surface and side views proved effective in locating the precise reaction sites.The partition layer showed a high degree of positive reaction.The thylakoid membrane proper also contained particles of positive reaction. The positive site extended to the thylakoid loculus to form protrusions.These results are in harmony with the localization of the PS-I complex particles on the PF face side of the thylakoid membrane as revealed by the freeze fracture technique.The concurrent microchemical and topochemical study of tetrazolium reduction by isolated Vicia chloroplasts under illumination has demonstrated that the photosystem responsible for the reduction is the PS-II*. It also revealed that the electron transfer activity mediated by this system is located in the thylakoid membrane proper, and extends to the surface of the loculus (12). Similar cytochemical study along this line was undertaken of the DAB oxidation by isolated Vicia chloroplasts under illumination in order to get some insight into the following three points : first, the photosystem responsible for the oxidation reaction under illumination, secondly, the possible role of endogenous active oxygen in the reaction, and thirdly, the localization of the photosystem concerned in the thylakoid membrane. This paper deals with the results obtained.

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Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Cytochemical study of diaminobenzidine oxidation by isolated Vicia chloroplasts under illumination.

Imaizumi

Hiraoka

1982

Acta Histochem. Cytochem

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“…With the exception of the outer sheath, the cells of DC-2 resembled the related genera Anabaena (12) and Microcystis (13) in structure. Cell profiles were 0.6-1.2 Im in width (average Abbreviations: PE, phycoerythrin; PUB, phycourobilin; PEB, phycoerythrobilin; CD, circular dichroism.…”

Section: Resultsmentioning

confidence: 96%

Morphology of a novel cyanobacterium and characterization of light-harvesting complexes from it: Implications for phycobiliprotein evolution

Kursar¹,

Swift²,

Alberte³

1981

Proc. Natl. Acad. Sci. U.S.A.

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The morphology of the marine cyanobacterium DC-2 and two light-harvesting complexes from it have been characterized. DC-2 has an outer cell wall sheath not previously observed, the purified phycoerythrin shows many unusual properties that distinguish it from all phycoerythrins characterized to date, and isolated phycobilisomes have a single absorption band at 640 nm in the phycocyanin-allophycocyanin region of the spectrum. On the basis of these observations we suggest that DC-2, rather than being a member of the Synechococcus group, should be placed in its own taxonomic group. In addition, the particular properties of the isolated phycoerythrin suggest that it may be representative of an early stage in the evolution of the phycoerythrins. These observations are of special interest in light of the contribution DC-2 and related cyanobacteria may make to global primary productivity. Several species of blue-green-and red-pigmented marine cyanobacteria that not only are abundant in the world's oceans but also may be responsible for a significant fraction ofprimary productivity have been discovered recently (1, 2). The red-pigmented cells have the virtue that they are readily distinguished from most other phytoplankton species by their principal in vivo fluorescence emission in the orange (560-580 nm), which undoubtedly arises from the presence ofthe red pigment-protein, phycoerythrin (PE). In some cyanobacteria and most red algae, PE serves as the major light-harvesting pigment for photosynthesis and is found in association with the other major phycobilipigments, phycocyanin and allophycocyanin. In vivo these phycobilipigments are aggregated into macromolecular arrays that form discrete organelles called phycobilisomes and are attached to the chlorophyll a-containing photosynthetic lamellae (3).Such an organization allows for excitation energy transfer from the shortest-wavelength-absorbing pigment, PE, to phycocyanin and allophycocyanin and ultimately to the chlorophyll a residing in the photochemical reaction centers ofphotosystems I and II (3-5). Therefore, the phycobilipigments serve two important functions in photosynthesis: (i) they increase photon capture under light-limited conditions and (ii) they increase the spectral range of light energy available for photosynthesis by absorbing light where chlorophyll a absorbs weakly and where there is the greatest transmission of light in the water column.Recent studies have demonstrated that the phycobiliproteins have highly conserved NH2-terminal sequences (6)(7)(8) and that phycobilisome structure is also fairly conservative (3). The dual requirements for efficient energy transfer from the phycobilipigments to chlorophyll a and for assembly of a phycobilisome seem to impose strong constraints on the nature ofthe phycobilipigments and their in vivo macromolecular organization.After examining the in vivo spectral properties of several of the recently discovered species ofcyanobacteria, it came to our attention that one of the PE-containing types termed DC-2 ...

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“…Oxidation of DAB occurs in the photosynthetic lamellae of blue-green algae and of chloroplasts in green algae and leaves of higher plants when incubation is done under high light intensity (Chua, 1972;Lauritis et al, 1975;Nir and Pease, 1972;Nir and Seligman, 1970). In the thylakoidal body and lamellae of developing chloroplasts of tobacco, staining is not due to photooxidation of DAB since these plastid components stained when tissues were incubated in the DAB medium in the dark.…”

Section: Chloroplast Development In Expanding Leaves-mentioning

confidence: 99%

Development and Cytochemistry of the Thylakoidal Body in Tobacco Chloroplasts

Hurkman

Kennedy

1977

American J of Botany

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Developing plastids in young tobacco leaves contain thylakoidal bodies, inclusions bound by a single membrane continuous with stroma lamellae. Both the thylakoidal body and its attached lamellae contain an enzyme that catalyzes an oxidation reaction with 3,3'‐diaminobenzidine (DAB). DAB staining of the thylakoidal body and lamellae is not the result of photo‐oxidation and is inhibited by potassium cyanide. The thylakoidal body disappears as plastids develop into chloroplasts and, further, the lamellar systems of the mature chloroplasts do not stain with DAB. In developing chloroplasts, it is suggested that the thylakoidal body forms by accumulation of protein which stains with DAB within primary lamellae derived from the inner plastid membrane. The ultrastructural and cytochemical evidence suggests that the thylakoidal body stores protein used later in lamellar formation.

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Photosynthetically-linked oxidation of diaminobenzidine in blue-green algae

Cited by 11 publications

References 21 publications

Cytochemical study of diaminobenzidine oxidation by isolated Vicia chloroplasts under illumination.

Cytochemical study of diaminobenzidine oxidation by isolated Vicia chloroplasts under illumination.

Morphology of a novel cyanobacterium and characterization of light-harvesting complexes from it: Implications for phycobiliprotein evolution

Development and Cytochemistry of the Thylakoidal Body in Tobacco Chloroplasts

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