Results 201 to 210 of about 10,615 (226)
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Long-chain flavodoxin FldB from Escherichia coli
Journal of Biomolecular NMR, 2014Flavodoxins are a family of small electron transferases widely distributed in prokaryotes. They utilize a noncovalently bound flavin mononucleotide (FMN) molecule as the redox center, and are able to switch between three different redox states, namely the oxidized (ox) state, the one-electron reduced semiquinone (sq) state, and the twoelectron reduced ...
Qian, Ye +3 more
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A constitutive flavodoxin from a eukaryotic alga
Biochemical and Biophysical Research Communications, 1978Abstract We report the isolation and some properties of a flavodoxin from a eukaryotic organism, the naturally occurring red alga Chondrus crispus . Unlike the situation with most other organisms the flavodoxin, under normal growth conditions, is the predominantly formed low-potential electron carrier, an accompanying ferredoxin occurring in ...
M P, Fitzgerald, A, Husain, L J, Rogers
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Biochemistry, 1990
Flavodoxins from Clostridium beijerinckii and from Megasphaera elsdenii with 1-carba-1-deaza-FMN substituted for FMN have been used to study flavin-protein interactions in flavodoxins. The oxidized 1-deaza analogue of FMN binds to apoflavodoxins from M. elsdenii and C. beijerinckii (a.k.a.
M L, Ludwig +4 more
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Flavodoxins from Clostridium beijerinckii and from Megasphaera elsdenii with 1-carba-1-deaza-FMN substituted for FMN have been used to study flavin-protein interactions in flavodoxins. The oxidized 1-deaza analogue of FMN binds to apoflavodoxins from M. elsdenii and C. beijerinckii (a.k.a.
M L, Ludwig +4 more
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Physicochemical properties of flavodoxin from Desulfovibrio vulgaris
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975Reductive titration curves of flavodoxin from Desulfovibrio vulgaris displayed two one-electron steps. The redox potential E-2 for the couple oxidized flavodoxin/flavodoxin semiquinone was determined by direct titration with dithionite. E-2 was -149 plus or minus 3 mV (pH 7.78, 25 degrees C).
M, Dubourdieu, J, le Gall, V, Favaudon
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Structure of oxidized flavodoxin from Anacystis nidulans
Journal of Molecular Biology, 1983The structure of oxidized flavodoxin from the cyanobacterium Anacystis nidulans has been determined at 2.5 A resolution with phases calculated from ethylmercury phosphate and dimercuriacetate derivatives. The determination of partial sequences, including a total of 85 residues, has assisted in the interpretation of the electron density.
W W, Smith +6 more
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[169] Flavodoxin of Clostridium pasteurianum
1971Publisher Summary Flavodoxin (Fld) is an electron-transferring flavoprotein isolated from extracts of Clostridium pasteurianum . It replaces the electron-transferring protein, bacterial ferredoxin (Fd), in the iron-deficient cell. Flavodoxin is isolated from extracts of Peptostreptococcus elsdenii and Desulfovibrio gigas .
E. Knight, R.W.F. Hardy
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Structural basis for energy and electron transfer of the photosystem I–IsiA–flavodoxin supercomplex
Nature Plants, 2020P. Cao +8 more
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Flavodoxins: sequence, folding, binding, function and beyond
Cellular and Molecular Life Sciences, 2006Flavodoxins are electron-transfer proteins involved in a variety of photosynthetic and non-photosynthetic reactions in bacteria, whereas, in eukaryotes, a descendant of the flavodoxin gene helps build multidomain proteins. The redox activity of flavodoxin derives from its bound flavin mononucleotide cofactor (FMN), whose intrinsic properties are ...
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