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Evidence for the presence of a [2Fe-2S]
ferredoxin in bean sprouts.
Biochim Biophys Acta 1988 Jul 6;934(2):169-76
Hirasawa M, Sung JD, Malkin R, Zilber A, Droux M, Knaff DB.
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock
79409-1061.
An iron-sulfur protein with properties similar to those of ferredoxins found in
the leaves of higher plants has been isolated from bean sprouts--a
non-photosynthetic plant tissue. The bean sprout protein has a molecular mass of
12.5 kDa and appears to contain a single [2Fe-2S] cluster. The absorbance and
circular dichroism spectra of the bean sprout protein resemble those of spinach
leaf ferredoxin and the bean sprout protein can replace spinach ferredoxin as an
electron donor for NADP+ reduction, nitrite reduction and thioredoxin reduction
by spinach leaf enzymes. Although the reduced bean sprout protein (Em = -440 mV)
is a slightly stronger reductant than spinach ferredoxin and appears to be less
acidic than spinach ferredoxin, the two proteins are similar enough so that the
bean sprout protein is recognized by an antibody raised against spinach
ferredoxin
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