The amino acid sequence of ferredoxin from the alga Mastigocladus laminosus

Hase, Toshiharu; Wakabayashi, Shigeo; Matsubara, Hiroshi; Rao, K. K.; Hall, D.O.; Widmer, Herbert; Gysi, Jürg R.; Zuber, Herbert

doi:10.1016/s0031-9422(00)88721-x

Cited by 21 publications

(10 citation statements)

References 29 publications

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“…elongatus , Sy. lividus (Borden & Margoliash, 1979), M. laminosus (Hase et al, 1978a) and C. caldarium (Hase et al, 1978b), and ferredoxins from mesophiles, Sp. platensis (Tanaka et al, 1976), A. Sacrum (Hase et al, 1976a), Anabaena 7120 vegetative cells (Alam et al, 1986), Anabaena 7120 heterocysts (Bo È hme & Haselkorn, 1988) and E. arvense (Hase et al, 1977) .…”

Section: Contribution Of Hydrophobic Interaction To Thermostabilitymentioning

confidence: 99%

Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

Hatanaka

Tanimura

Katoh

et al. 1997

Journal of Molecular Biology

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Section: Contribution Of Hydrophobic Interaction To Thermostabilitymentioning

confidence: 99%

Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

Hatanaka

Tanimura

Katoh

et al. 1997

Journal of Molecular Biology

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“…7 Fd isolated from the thermophilic cyanobacterium Mastigocladus laminosus (mFd), has been shown to display thermostable properties, with maximal activity at 65 8C. 8 Although the thermostability of mFd was discovered more than 20 years ago, 8 its determinants remain unsolved. The factors that determine thermostability in proteins are under considerable investigation.…”

Section: Introductionmentioning

confidence: 99%

Structural Basis for the Thermostability of Ferredoxin from the Cyanobacterium Mastigocladus laminosus

Fish

Danieli

Ohad

et al. 2005

Journal of Molecular Biology

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“…Finally, the Berkley strain of Nostoc muscorum was recently identified as A. variabilis (27). The amino acid sequence of the major ferredoxin component (ferredoxin I by convention [34]) of N. muscorum (14), which was deter- (Fig. 4).…”

Section: Resultsmentioning

confidence: 99%

Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120

Alam¹,

Whitaker²,

Krogmann³

et al. 1986

J Bacteriol

107

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The structural gene for ferredoxin I, petF, from the cyanobacterium Anabaena sp. strain PCC 7120 has been isolated from a recombinant lambda library. Mixtures of tetradecanucleotides and heptadecanucleotides, each containing all possible DNA sequences corresponding to two separate regions of the ferredoxin amino acid sequence, were synthesized and used as hybridization probes to identify a genomic clone containing the coding sequence for the petF gene. The sequence of the entire petF coding region and portions of the 3'-and 5'-flanking regions was determined. The DNA sequence of petF suggests that, in contrast to the nucleus-encoded plant protein, cyanobacterial apoferredoxin is not synthesized as a higher-molecular-weight precursor. The Anabaena petF gene is a single-copy gene. During growth on complete medium it was transcribed into a monocistronic mRNA species of approximately 500 bases that initiated 100 base pairs upstream from the petF coding region.Ferredoxin is an acidic, nonheme, iron-sulfur protein with a wide distribution in organisms ranging from nonphotosynthetic, anaerobic bacteria to higher plants and animals. In plants and cyanobacteria, ferredoxin is recognized primarily as a component of the photosynthetic electron transport chain (31). In addition to its central role in NADP+ reduction and cyclic photophosphorylation, ferredoxin functions, directly or indirectly, in a variety of biological electron transfer systems. These include such diverse processes as nitrogen fixation (38), sulfate-sulfite reduction (32), nitrate-nitrite reduction (17, 25), and glutamate synthesis (17). Furthermore, ferredoxin is responsible, via the ferredoxinthioredoxin system, for the regulation of enzymes involved in photosynthetic carbon metabolism (3).Two distinct molecular forms of ferredoxin have been identified in some plants and cyanobacteria. The primary structure of ferredoxins I and II from a number of organisms has been determined (for a compilation, see references 12 and 21), and the amino acid sequence data suggest that these two ferredoxins arose via gene duplication (21). At present, however, no functional differences have been attributed to this dimorphism. Aside from ferredoxins I and II, some cyanobacteria apparently contain yet another form of this protein. Cohn et al. (6) have isolated a membrane-associated ferredoxin from the cyanobacterium Aphanizomenon flosaquae that is distinct from ferredoxin I with regard to location within the cell, chromatographic behavior on a DEAE-cellulose column, and electron spin resonance spectra. The limited amino acid sequence data suggest that the membrane-associated ferredoxin is more similar to ferredoxin I than most ferredoxin II molecules are to ferredoxin

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The amino acid sequence of ferredoxin from the alga Mastigocladus laminosus

Cited by 21 publications

References 29 publications

Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

Structural Basis for the Thermostability of Ferredoxin from the Cyanobacterium Mastigocladus laminosus

Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120

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