Structure-function studies of [2Fe-2S] ferredoxins

@article{Holden1994StructurefunctionSO,
  title={Structure-function studies of [2Fe-2S] ferredoxins},
  author={Hazel M. Holden and Bruce L. Jacobson and John K. Hurley and Gordon Tollin and Byung-Ha Oh and Lars Skjeldal and Young Kee Chae and H. Q. Cheng and Bin Xia and John L. Markley},
  journal={Journal of Bioenergetics and Biomembranes},
  year={1994},
  volume={26},
  pages={67-88}
}
The ability to overexpress [2Fe-2S] ferredoxins inEscherichia coli has opened up exciting research opportunities. High-resolution x-ray structures have been determined for the wild-type ferredoxins produced by the vegetative and heterocyst forms ofAnabaena strain 7120 (in their oxidized states), and these have been compared to structural information derived from multidimensional, multinuclear NMR spectroscopy. The electron delocalization in these proteins in their oxidized and reduced states… 
Multinuclear Magnetic Resonance and Mutagenesis Studies of Structure-Function Relationships in [2Fe-2S] Ferredoxins
Iron-sulfur proteins are present in virtually all living organisms. Their function is to transfer electrons to various partners. They have iron and sulfur in their chromophore and rather low
Structure and Function of Plant-Type Ferredoxins
TLDR
The plant-type ferredoxins have come to a new era in which different roles of Fds and interactions with various enzymes are clarified on the basis of the tertiary and quaternary structures, although they are premature at present.
An electrochemical, kinetic, and spectroscopic characterization of [2Fe-2S] vegetative and heterocyst ferredoxins from Anabaena 7120 with mutations in the cluster binding loop.
TLDR
These studies suggest that residues 48 and 78 are involved in the pathway of electron transfer between VFd and FNR and/or that mutations at these positions induce a unique, but unproductive orientation of the two proteins within the protein-protein complex.
Vertebrate-type and plant-type ferredoxins: crystal structure comparison and electron transfer pathway modelling.
TLDR
Model calculations suggest that FE1 is the origin of electron transfer pathways to the surface in all analyzed [2Fe-2S] ferredoxins and that additional transfer probability for electrons tunneling from the more buried FE2 to the cysteine residue in position 92 of Adx is present in some.
Expression, Purification, and Characterization of a [Fe2S2] Cluster Containing Ferredoxin from Acidithiobacillus ferrooxidans
TLDR
The MALDI-TOF MS and spectra results of the recombinant protein confirmed that the iron–sulfur cluster was correctly inserted into the active site of the protein and site-directed mutagenesis results revealed that Cys42, Cys48, CYS51, and Cys87 were ligating with the [Fe2S2] cluster of theprotein.
Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase.
TLDR
Results provide strong support for the proposal that all three clusters are located in the FrdB subunit, and the redox and spectroscopic properties of the [2Fe-2S] and [3Fe-4S] clusters are unchanged compared to the wild-type enzyme.
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References

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Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution.
The [2Fe-2S] ferredoxin produced in the heterocyst cells of Anabaena 7120 plays a key role in nitrogen fixation, where it serves as an electron acceptor from various sources and an electron donor to
Structure of S. platensis [2Fe-2S] ferredoxin and evolution of chloroplast-type ferredoxins
TLDR
The three-dimensional structure of a [2Fe-2S] ferredoxin of Spirulina platensis, a blue-green alga, determined by X-ray crystallography at 2.5 Å resolution is reported and the characteristic features of the molecule are discussed in relation to the molecular evolution of ferredoxins of this class.
Optical, EPR, and 1H NMR spectroscopy of serine-ligated [2Fe-2S] ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin.
TLDR
The EPR and NMR results obtained here reveal that mutant Cys46Ser has a "plant-type" cluster but that mutants Cys49Ser hasA "vertebrate- type" cluster.
Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120.
The molecular structure of the oxidized form of the (2Fe-2S) ferredoxin isolated from the cyanobacterium Anabaena s ecies strain PCC 7 120 has been determined by X-ray diffraction analysis to
Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120.
The molecular structure of the oxidized form of the [2Fe-2S] ferredoxin isolated from the cyanobacterium Anabaena species strain PCC 7120 has been determined by X-ray diffraction analysis to a
Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli.
Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli.
  • V. Coghlan, L. Vickery
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1989
TLDR
A cDNA fragment encoding human ferredoxin, a mitochondrial [2Fe-2S] protein, was introduced into Escherichia coli by using an expression vector based on the approach of Nagai and Thøgersen and should be useful in production of native and structurally altered forms of human fer redoxin for studies of ferred toxin structure and function.
Identification of localized redox states in plant-type two-iron ferredoxins using the nuclear Overhauser effect.
TLDR
The homonuclear Overhauser effect has been employed to assign the contact-shifted resonances for the reduced form of two typical plant-type two-iron ferredoxins from the algae Spirulina platensis and Porphyra umbilicalis, demonstrating that the NOE should have broad general applicability for the assignments and electronic structural elucidation of diverse subclasses of paramagnetic iron-sulfur cluster proteins.
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