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
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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“Fe-S clusters are ubiquitous, inorganic co-factors that contribute to a wide range of cellular pathways from genome integrity and gene regulation to energy production and immune responses, and are required for numerous biological functions, particularly enzymatic activity (Beinert, 2000; Johnson et al., 2005; Lee et al., 2009; Fuss et al., 2015).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Johnson et al., 2005
In the citing paper
“iron can act alone or in iron–sulfur clusters as a prosthetic moiety for members of the oxidoreductase, nitrogenase, hydrogenase, dehydrogenase, and hydratase enzyme families [7–12].”
From Heme Synthesis and Acquisition in Bacterial Pathogens (2016) · cites this paper as [11]
Citations
Cites
Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
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Iron-sulfur clusters: nature's modular, multipurpose structures
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Activated Acetic Acid by Carbon Fixation on (Fe,Ni)S Under Primordial Conditions
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The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
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Iron-sulfur proteins: ancient structures, still full of surprises
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Assembly of Iron-Sulfur Clusters
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Density-Functional Theory of Spin Polarization and Spin Coupling in Iron—Sulfur Clusters
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Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation
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Cited by
Sorted by citations
Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
Vignais, P. M., & Billoud, B. (2007) · Chemical Reviews · doi:10.1021/cr050196r · Cited by 1,617
Structure/Function Relationships of [NiFe]- and [FeFe]-Hydrogenases
Fontecilla-Camps, J. C., Volbeda, A., Cavazza, C., & Nicolet, Y. (2007) · Chemical Reviews · doi:10.1021/cr050195z · Cited by 1,365
Function and biogenesis of iron-sulphur proteins
Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167
The role of iron regulatory proteins in mammalian iron homeostasis and disease
Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055
“Mammalian iron-sulfur cluster assembly Assembly of iron-sulfur clusters is a complex process involving many enzymes and scaffold protein”
BackgroundRegulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
Metadata
- 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
- 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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