Zobrazeno 1 - 10
of 28
pro vyhledávání: '"S. I. Beale"'
Autor:
S. M. Mayer, S. Y. Grooms, Jon D. Weinstein, R. W. Howell, S. I. Beale, R. D. Leverette, P. S. Brignola
Publikováno v:
Plant Physiology. 101:657-665
In plants, algae, and many bacteria, the heme and chlorophyll precursor, [delta]-aminolevulinic acid (ALA), is synthesized from glutamate in a reaction involving a glutamyl-tRNA intermediate and requiring ATP and NADPH as cofactors. In particulate-fr
Publikováno v:
Journal of Bacteriology. 172:7071-7084
Salmonella typhimurium forms the heme precursor delta-aminolevulinic acid (ALA) exclusively from glutamate via the five-carbon pathway, which also occurs in plants and some bacteria including Escherichia coli, rather than by ALA synthase-catalyzed co
Autor:
S. I. Beale
It should be noted that the focus of the research changed somewhat during the course of the current award. The initial focus is indicated by the title of the current grant, ''The Magnesium Branch of the Chlorophyll Biosynthetic Pathway''. During the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a534534b02b10ca51ad7de616ab1f45a
https://doi.org/10.2172/833881
https://doi.org/10.2172/833881
Publikováno v:
Plant molecular biology. 43(1)
The phytobilin chromophores of phycobiliproteins and phytochromes are biosynthesized from heme in a pathway that begins with the opening of the tetrapyrrole macrocycle of protoheme to form biliverdin IXalpha, in a reaction catalyzed by heme oxygenase
Publikováno v:
Plant molecular biology. 39(2)
Expression of the Chlamydomonas reinhardtii gsa gene encoding the chlorophyll biosynthetic enzyme glutamate 1-semialdehyde aminotransferase was previously shown to be induced by blue light. Possible blue light photoreceptors include flavins and carot
Autor:
G, Rhie, S I, Beale
Publikováno v:
The Journal of biological chemistry. 269(13)
Cyanobacteria, red algae, and cryptophytes contain phycobiliproteins which function as photosynthetic light-harvesting pigments. The chromophores of phycobiliproteins are phycobilins, open-chain tetrapyrroles that are synthesized from protoheme. The
Autor:
S I, Beale
Publikováno v:
Ciba Foundation symposium. 180
Phycobilins are open-chain tetrapyrroles of plants and algae which act as the chromophores of phycobiliproteins where they function as light energy-harvesting pigments. Phytochromobilin, another open-chain tetrapyrrole, is the chromophore of phytochr
Autor:
G, Rhie, S I, Beale
Publikováno v:
The Journal of biological chemistry. 267(23)
The unicellular red alga, Cyanidium caldarium, synthesizes phycocyanobilin from protoheme via biliverdin IX alpha. In vitro transformation of protoheme to biliverdin IX alpha and biliverdin IX alpha to phycobilins were previously shown to require NAD
Publikováno v:
The Journal of biological chemistry. 267(21)
The unicellular rhodophyte, Porphyridium cruentum, and the filamentous cyanobacterium, Calothrix sp. PCC 7601, contain phycobiliproteins that have covalently bound phycobilin chromophores. Overnight incubation of solvent-extracted cells at 40 degrees
Autor:
S I, Beale, J, Cornejo
Publikováno v:
The Journal of biological chemistry. 266(33)
A partially purified protein fraction from the phycocyanin-containing unicellular rhodophyte, Cyanidium caldarium, reductively transforms biliverdin IX alpha to a violet colored bilin in the presence of NADPH, ferredoxin, and ferredoxin-NADP+ reducta