Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in Azotobacter vinelandii

JS Martin del Campo, J Rigsbee… - Critical Reviews in …, 2022 - Taylor & Francis
Understanding how Nature accomplishes the reduction of inert nitrogen gas to form
metabolically tractable ammonia at ambient temperature and pressure has challenged …

The interactions of molecular chaperones with client proteins: why are they so weak?

T Arhar, A Shkedi, CM Nadel, JE Gestwicki - Journal of Biological Chemistry, 2021 - ASBMB
The major classes of molecular chaperones have highly variable sequences, sizes, and
shapes, yet they all bind to unfolded proteins, limit their aggregation, and assist in their …

Molecular mechanism of ISC iron–sulfur cluster biogenesis revealed by high-resolution native mass spectrometry

CW Lin, JW McCabe, DH Russell… - Journal of the …, 2020 - ACS Publications
Iron–sulfur (Fe–S) clusters are ubiquitous protein cofactors that are required for many
important biological processes including oxidative respiration, nitrogen fixation, and …

Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron–sulfur cluster assembly

SP Bennett, JC Crack, R Puglisi, A Pastore… - Chemical …, 2023 - pubs.rsc.org
Iron–sulfur (Fe–S) clusters are cofactors essential for life. Though the proteins that function
in the assembly of Fe–S clusters are well known, details of the molecular mechanism are …

[HTML][HTML] Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron–sulfur cluster biosynthesis and delivery

JL Markley, JH Kim, Z Dai, JR Bothe, K Cai… - FEBS letters, 2013 - Elsevier
IscU from Escherichia coli, the scaffold protein for iron-sulfur cluster biosynthesis and
delivery, populates a complex energy landscape. IscU exists as two slowly interconverting …

Interaction of client—the scaffold on which FeS clusters are build—with J-domain protein Hsc20 and its evolving Hsp70 partners

J Marszalek, EA Craig - Frontiers in Molecular Biosciences, 2022 - frontiersin.org
In cells molecular chaperone systems consisting of Hsp70 and its obligatory J-domain
protein (JDP) co-chaperones transiently interact with a myriad of client proteins—with JDPs …

Chaperone function in Fe–S protein biogenesis: Three possible scenarios.

J Marszalek, EA Craig, M Pitek, R Dutkiewicz - Biochimica et Biophysica …, 2024 - Elsevier
Among the six known iron‑sulfur (Fesingle bondS) cluster biogenesis machineries that
function across all domains of life only one involves a molecular chaperone system. This …

Mechanism of mitochondrial [2Fe2S] cluster biosynthesis

K Want, B D'Autréaux - Biochimica et Biophysica Acta (BBA)-Molecular Cell …, 2024 - Elsevier
Iron‑sulfur (Fesingle bondS) clusters constitute ancient cofactors that accompany a versatile
range of fundamental biological reactions across eukaryotes and prokaryotes. Several …

Role of IscX in Iron–Sulfur Cluster Biogenesis in Escherichia coli

JH Kim, JR Bothe, RO Frederick… - Journal of the …, 2014 - ACS Publications
The Escherichia coli isc operon encodes key proteins involved in the biosynthesis of iron–
sulfur (Fe–S) clusters. Whereas extensive studies of most ISC proteins have revealed their …

Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) …

K Cai, RO Frederick, JH Kim, NM Reinen… - Journal of Biological …, 2013 - ASBMB
Background: Iron-sulfur cluster biosynthesis involves a scaffold protein (ISCU), cysteine
desulfurase (NFS1), chaperone (mtHSP70), and co-chaperone (HSC20). Results: Human …