Structural, mechanistic and coordination chemistry of relevance to the biosynthesis of iron–sulfur and related iron cofactors☆

Qi, Wenbin; Cowan, J. A.

doi:10.1016/j.ccr.2010.10.016

Cited by 35 publications

(25 citation statements)

References 151 publications

(255 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is in contrast to our cluster containing control protein Yah1, which has a 4 cysteine coordination environment ligating its tightly bound FeS cluster. 49 Finally, iron-ligand bond lengths we observe are similar to those reported for Fe(II)-binding proteins from other biological systems 50, 51 and to bond lengths we previously reported for yIsu1. 15 …”

Section: Discussionsupporting

confidence: 88%

In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation

et al. 2017

View full text Add to dashboard Cite

FeS-clusters are utilized by numerous proteins within several biological pathways that are essential for life. In eukaryotes, the primary FeS-cluster production pathway is the mitochondrial iron-sulfur cluster (ISC) pathway. In Saccharomyces cerevisiae, de novo FeS-cluster formation is accomplished through coordinated assembly with the substrates iron and sulfur by the scaffold assembly protein “Isu1”. Sulfur for cluster assembly is provided by cysteine desulfurase “Nfs1”, a protein that works in union with its accessory protein “Isd11”. Frataxin “Yfh1” helps direct cluster assembly by serving as a modulator of Nfs1 activity, by assisting in the delivery of sulfur and Fe(II) to Isu1, or more likely through a combination of these and other possible roles. In vitro studies on the yeast ISC machinery have been limited, however, due to the inherent instability of recombinant Isu1. Isu1 is a molecule prone to degradation and aggregation. To circumvent Isu1 instability, we have replaced yeast Isu1 with the fly ortholog to stabilize our in vitro ISC assembly system and assist us in elucidating molecular details of the yeast ISC pathway. Our laboratory previously observed that recombinant frataxin from Drosophila melanogaster has remarkable stability compared to the yeast ortholog. Here we provide the first characterization of D. melanogaster Isu1 (fIscU) and demonstrate its ability to function within the yeast ISC machinery both in vivo and in vitro. Recombinant fIscU has similar physical properties similar to that of yeast Isu1. It functions as a stable dimer with similar Fe(II) affinity and ability to form two 2Fe-2S clusters as the yeast dimer. The fIscU and yeast ISC proteins are compatible in vitro; addition of Yfh1 to Nfs1-Isd11 increases the rate of FeS-cluster formation on fIscU to a similar extent observed with Isu1. Finally, fIscU expressed in mitochondria of a yeast strain lacking Isu1 (and its paralog Isu2) is able to completely reverse the deletion phenotypes. These results demonstrate fIscU can functionally replace yeast Isu1 and it can serve as a powerful tool for exploring molecular details within the yeast ISC pathway.

show abstract

Section: Discussionsupporting

confidence: 88%

In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation

et al. 2017

View full text Add to dashboard Cite

show abstract

“…The Fe-S proteins contain inorganic iron and sulfur as cofactors (40,47,48). Iron and sulfur are redox active, and the cluster can undergo redox reactions under physiological conditions.…”

Section: Discussionmentioning

confidence: 99%

FeoC from Klebsiella pneumoniae Contains a [4Fe-4S] Cluster

Hsueh

Chen

et al. 2013

J Bacteriol

View full text Add to dashboard Cite

Iron is essential for pathogen survival, virulence, and colonization. Feo is suggested to function as the ferrous iron (Fe 2؉ ) transporter. The enterobacterial Feo system is composed of 3 proteins: FeoB is the indispensable component and is a large membrane protein likely to function as a permease; FeoA is a small Src homology 3 (SH3) domain protein that interacts with FeoB; FeoC is a winged-helix protein containing 4 conserved Cys residues in a sequence suitable for harboring a putative iron-sulfur (Fe-S) cluster. The presence of an iron-sulfur cluster on FeoC has never been shown experimentally. We report that under anaerobic conditions, the recombinant Klebsiella pneumoniae FeoC (KpFeoC) exhibited hyperfine-shifted nuclear magnetic resonance (NMR) and a UV-visible (UV-Vis) absorbance spectrum characteristic of a paramagnetic center. The electron paramagnetic resonance (EPR) and extended X-ray absorption fine structure (EXAFS) results were consistent only with the [4Fe-4S] clusters. Substituting the cysteinyl sulfur with oxygen resulted in significantly reduced cluster stability, establishing the roles of these cysteines as the ligands for the Fe-S cluster. When exposed to oxygen, the [4Fe-4S] cluster degraded to [3Fe-4S] and eventually disappeared. We propose that KpFeoC may regulate the function of the Feo transporter through the oxygen-or iron-sensitive coordination of the Fe-S cluster.

show abstract

“…In the cell, however, an extensive machinery has evolved for the formation and incorporation of specific iron-sulfur centers into proteins. It has been shown that the sulfur in iron-sulfur centers originates from cysteine thiol and is transferred as S 0 bound to the sulfurtransferase component in both prokaryotic and eukaryotic systems [222]. …”

Section: H2s Reaction With Metalsmentioning

confidence: 99%

Chemical foundations of hydrogen sulfide biology

2013

View full text Add to dashboard Cite

Following nitric oxide (nitrogen monoxide) and carbon monoxide, hydrogen sulfide (or its newer systematic name sulfane, H2S) became the third small molecule that can be both toxic and beneficial depending on the concentration. In spite of its impressive therapeutic potential, the underlying mechanisms for its beneficial effects remain unclear. Any novel mechanism has to obey fundamental chemical principles. H2S chemistry was studied long before its biological relevance was discovered, however, with a few exceptions, these past works have received relatively little attention in the path of exploring the mechanistic conundrum of H2S biological functions. This review calls attention to the basic physical and chemical properties of H2S, focuses on the chemistry between H2S and its three potential biological targets: oxidants, metals and thiol derivatives, discusses the applications of these basics into H2S biology and methodology, and introduces the standard terminology to this youthful field.

show abstract

Structural, mechanistic and coordination chemistry of relevance to the biosynthesis of iron–sulfur and related iron cofactors☆

Cited by 35 publications

References 151 publications

In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation

In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation

FeoC from Klebsiella pneumoniae Contains a [4Fe-4S] Cluster

Chemical foundations of hydrogen sulfide biology

Contact Info

Product

Resources

About