Cited by 1,438Metalloenzymes and iron-sulfur proteinsEnzyme Structure and FunctionInorganic Chemistry and Materials

The DOI matches its Crossref record; 209 of the 209 references it cites were found in a registry or an index.

STRUCTURE, FUNCTION, AND FORMATION OF BIOLOGICAL IRON-SULFUR CLUSTERS

Johnson, Deborah C., Dean, Dennis R., Smith, Archer D., Johnson, Michael K.·2005·Annual Review of Biochemistry

DOI 10.1146/annurev.biochem.74.082803.133518

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Abstract

Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic groups that are required to sustain fundamental life processes. Owing to their remarkable structural plasticity and versatile chemical/electronic features [Fe-S] clusters participate in electron transfer, substrate binding/activation, iron/sulfur storage, regulation of gene expression, and enzyme activity. Formation of intracellular [Fe-S] clusters does not occur spontaneously but requires a complex biosynthetic machinery. Three different types of [Fe-S] cluster biosynthetic systems have been discovered, and all of them are mechanistically unified by the requirement for a cysteine desulfurase and the participation of an [Fe-S] cluster scaffolding protein. Important mechanistic questions related to [Fe-S] cluster biosynthesis involve the molecular details of how [Fe-S] clusters are assembled on scaffold proteins, how [Fe-S] clusters are transferred from scaffolds to target proteins, how various accessory proteins participate in [Fe-S] protein maturation, and how the biosynthetic process is regulated.

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10.1074/jbc.275.12.8283 · DOI
10.1074/jbc.M104067200 · DOI

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Miller, H. K., & Auerbuch, V. (2015) · Metallomics · doi:10.1039/c5mt00012b · Cited by 60
Biogenesis of Fe/S proteins and pathogenicity: IscR plays a key role in allowing Erwinia chrysanthemi to adapt to hostile conditions
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“Scaffolds in each system are referred to as NifU, IscANif, IscU, IscA and SufA (Barras et al., 2005; Fontecave et al., 2005; Johnson et al., 2005a).”
BackgroundMethodInfluential
Photobiokatalyse: Aktivierung von Redoxenzymen durch direkten oder indirekten Transfer photoinduzierter Elektronen
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“FDX1 produces a market effect on steroidogenesis, while FDX2 is involved in the synthesis of Fe -S cluster and heme A (15).”
Background
The Role of CyaY in Iron Sulfur Cluster Assembly on the E. coli IscU Scaffold Protein
Iannuzzi, C., Adinolfi, S., Howes, B. D., García‐Serres, R., Clémancey, M., Latour, J., Smulevich, G., & Pastore, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021992 · Cited by 55
“Best known for their role in the oxidation-reduction reactions of the mitochondrial electron transport chain, Fe-S clusters have many other functions, which include generation of radicals, gene expression regulation and biosynthesis of sulfur derivatives [4,6].”
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“[Fe-S] clusters are typically coordinated by cysteine residues (41, 42), and we obtained evidence that the [4Fe-4S] cluster in UbiV is coordinated by four conserved cysteines arranged in a CXnCX12CX3C motif (Fig.”
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Analysis of Iron and Iron-Interacting Protein Dynamics During T-Cell Activation
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“Fe-S cluster interacting proteins are extremely diverse and include proteins involved in Fe-S cluster synthesis itself, mitochondrial respiration and DNA synthesis (12, 15).”
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Human ISCA1 Interacts with IOP1/NARFL and Functions in Both Cytosolic and Mitochondrial Iron-Sulfur Protein Biogenesis
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“Proteins with bound iron-sulfur clusters form an ancient and essential part of the proteome in every organism. Iron-sulfur proteins primarily transfer electrons in various biochemical processes, and they also take roles in substrate binding, iron-sulfur storage, gene regulation and enzyme activity”
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Nicotinamide nucleotide transhydrogenase regulates mitochondrial metabolism in NSCLC through maintenance of Fe-S protein function
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“Fe-S cluster biosynthesis occurs at a multiprotein complex consisting in part of the cysteine desulfurase (NFS1) and Fe-S scaffold protein (ISCU; Johnson et al., 2005).”
Background
Role of conserved cysteines in mediating sulfur transfer from IscS to IscU
Smith, A. D., Jeverson Frazzon, B., Dean, D. R., & Johnson, M. K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.046 · Cited by 54
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“Formation of Fe–S clusters is not a spontaneous process; a complex biosynthetic assembly machinery is required (29,39).”
Background
Genes for iron–sulphur cluster assembly are targets of abiotic stress in rice, O ryza sativa
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“The [4Fe-4S] cluster reportedly has various roles, such as in stabilization of the protein structure, as an electron donor, for substrate binding, and for enzymatic reactions (35).”
Background
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“Ferredoxin (Fd), IspG, IspH (involved in isoprenoid biosynthesis), LipA (lipoic acid synthase) and MiaB (tRNA methylthiotransferase) are apicoplast-targeted proteins which require [Fe–S] clusters as do members of the mitochondrial electron transport chain such as the Rieske protein, a subunit of succinate dehydrogenas…”
Background
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“S clusters (reviewed in Johnson et al., 2005).”
Comparative proteomic analysis of indica and japonica rice varieties
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“The SufB protein is a [4Fe-4S] protein (Layer et al., 2007) with an important role in photosynthetic electron transport, biosynthetic and metabolic reactions and the regulation of gene expression (Johnson et al., 2005).”
Background
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Raman spectroscopy a promising technique for investigations of metallothioneins
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“Bacteria possess at least three different pathways for iron-sulfur clusters biosynthesis [270-275].”
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A De Novo Designed 2[4Fe-4S] Ferredoxin Mimic Mediates Electron Transfer
Roy, A., Sommer, D. J., Schmitz, R. A., Brown, C. L., Gust, D., Astashkin, A. V., & Ghirlanda, G. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510621e · Cited by 51
Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis
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“The most common Fe-S clusters are [2Fe-2S] and [4Fe-4S] clusters, which are essential players in a variety of biological processes (Crack et al., 2012; Johnson et al., 2005; Lill, 2009).”
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“28 –30 Nevertheless, while promoting functional diversity, this variety in cluster coordination makes predictions of Fe-S cluster binding and consequently identification of new Fe-S proteins particularly difficult.”
Background
Advanced paramagnetic resonance spectroscopies of iron–sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)
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“Furthermore, organisms such as Mycobacterium tuberculosis, as well as some archaea, appear to possess only the Suf pathway for cluster assembly (AyalaCastro et al. 2008; Johnson et al. 2005).”
Background
Structural Analysis of Metal Sites in Proteins: Non-heme Iron Sites as a Case Study
Andreini, C., Bertini, I., Cavallaro, G., Najmanovich, R., & Thornton, J. M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.02.052 · Cited by 52
“4b) because the iron–sulfur clusters have various functions in addition to their typical role in electron transfer.(24,25) N- and O-donor ligands (mostly His and Asp or Glu) are prevalent in non-iron–sulfur sites, where they are typically (in 26 of 38 cases) found in combination.”
Background
Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU)
Kim, J. H., Tonelli, M., Frederick, R. O., Chow, D. C.-F., & Markley, J. L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.352617 · Cited by 50
“In the Fe-S cluster system for Fe-S cluster biosynthesis and delivery, which is conserved from prokaryotes (1) to the mitochondria of eukaryotes (2), Fe-S clusters are assembled on the scaffold protein IscU and are transferred to acceptor proteins through the agency of HscB, a J-protein co-chaperone, and HscA, a speci…”
Background
Crystal structure of Escherichia coli SufA involved in biosynthesis of iron–sulfur clusters: Implications for a functional dimer
Wada, K., Hasegawa, Y., Gong, Z., Minami, Y., Fukuyama, K., & Takahashi, Y. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.10.046 · Cited by 50

Authors: Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K.
Affiliations: Virginia Tech (US)
University of Georgia (US)
ORCID: Dean, Dennis R.
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 2005-06-01
Volume: 74
Issue: 1
Pages: 247-281
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.biochem.74.082803.133518
OpenAlex: W2116472408
Cited by: 1,438
References: 209
Citations by year: 2026: 48 · 2025: 68 · 2024: 57 · 2023: 62 · 2022: 75 · 2021: 94 · 2020: 64 · 2019: 67 · 2018: 65 · 2017: 72 · 2016: 64 · 2015: 63 · 2014: 73 · 2013: 69 · 2012: 74
FWCI: 7.17
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM62524)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Physical Sciences › Chemistry › Inorganic Chemistry › Inorganic Chemistry and Materials
Keywords: iron-sulfur clusters, Fe-S cluster biosynthesis, cysteine desulfurase, cluster assembly, protein maturation, electron transfer, prosthetic groups, gene expression regulation, enzyme activity
MeSH terms: Amino Acid Sequence, Bacterial Proteins, Carrier Proteins, Escherichia coli, Genes, Bacterial, Iron-Sulfur Proteins, Molecular Sequence Data, Nitrogenase, Protein Processing, Post-Translational, Sequence Homology, Amino Acid, Escherichia coli Proteins

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STRUCTURE, FUNCTION, AND FORMATION OF BIOLOGICAL IRON-SULFUR CLUSTERS

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