The origin and diversification of mitochondria

AJ Roger, SA Muñoz-Gómez, R Kamikawa - Current Biology, 2017 - cell.com
Mitochondria are best known for their role in the generation of ATP by aerobic respiration.
Yet, research in the past half century has shown that they perform a much larger suite of …

Mechanisms of mitochondrial iron-sulfur protein biogenesis

R Lill, SA Freibert - Annual review of biochemistry, 2020 - annualreviews.org
Mitochondria are essential in most eukaryotes and are involved in numerous biological
functions including ATP production, cofactor biosyntheses, apoptosis, lipid synthesis, and …

Functional spectrum and specificity of mitochondrial ferredoxins FDX1 and FDX2

V Schulz, S Basu, SA Freibert, H Webert, L Boss… - Nature chemical …, 2023 - nature.com
Ferredoxins comprise a large family of iron–sulfur (Fe–S) proteins that shuttle electrons in
diverse biological processes. Human mitochondria contain two isoforms of [2Fe-2S] …

[HTML][HTML] Mechanistic concepts of iron-sulfur protein biogenesis in Biology

JJ Braymer, SA Freibert, M Rakwalska-Bange… - Biochimica et Biophysica …, 2021 - Elsevier
Abstract Iron-sulfur (Fe/S) proteins are present in virtually all living organisms and are
involved in numerous cellular processes such as respiration, photosynthesis, metabolic …

Iron–sulfur cluster biogenesis and trafficking in mitochondria

JJ Braymer, R Lill - Journal of Biological Chemistry, 2017 - ASBMB
The biogenesis of iron–sulfur (Fe/S) proteins in eukaryotes is a multistage,
multicompartment process that is essential for a broad range of cellular functions, including …

FDX1 regulates cellular protein lipoylation through direct binding to LIAS

MB Dreishpoon, NR Bick, B Petrova, DM Warui… - Journal of Biological …, 2023 - ASBMB
Ferredoxins are a family of iron–sulfur (Fe-S) cluster proteins that serve as essential electron
donors in numerous cellular processes that are conserved through evolution. The …

Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin

S Gervason, D Larkem, AB Mansour… - Nature …, 2019 - nature.com
Abstract Iron-sulfur (Fe-S) clusters are essential protein cofactors whose biosynthetic defects
lead to severe diseases among which is Friedreich's ataxia caused by impaired expression …

Cytonuclear integration and co-evolution

DB Sloan, JM Warren, AM Williams, Z Wu… - Nature Reviews …, 2018 - nature.com
The partitioning of genetic material between the nucleus and cytoplasmic (mitochondrial and
plastid) genomes within eukaryotic cells necessitates coordinated integration between these …

Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex

MT Boniecki, SA Freibert, U Mühlenhoff, R Lill… - Nature …, 2017 - nature.com
Abstract Iron–sulfur (Fe/S) clusters are essential protein cofactors crucial for many cellular
functions including DNA maintenance, protein translation, and energy conversion. De novo …

[HTML][HTML] METTL17 is an Fe-S cluster checkpoint for mitochondrial translation

T Ast, Y Itoh, S Sadre, JG McCoy, G Namkoong… - Molecular cell, 2024 - cell.com
Friedreich's ataxia (FA) is a debilitating, multisystemic disease caused by the depletion of
frataxin (FXN), a mitochondrial iron-sulfur (Fe-S) cluster biogenesis factor. To understand the …