An enzyme having the samel-cysteine desulfurization activity previously described for the
NifS protein was purified from a strain ofAzotobacter vinelandii deleted for the nifSgene. This …

ABSTRACT A system for the controlled expression of genes in Azotobacter vinelandii by
using genomic fusions to the sucrose catabolic regulon was developed. This system was …

Iron-sulfur clusters ([Fe-S] clusters) are assembled on molecular scaffolds and subsequently
used for maturation of proteins that require [Fe-S] clusters for their functions. Previous …

The NifS and NifU proteins from Azotobacter vinelandii are required for the full activation of
nitrogenase. NifS is a homodimeric cysteine desulfurase that supplies the inorganic sulfide …

Genetic studies of bacteria and eukaryotes have led to identification of several gene
products that are involved in the biosynthesis of protein-bound iron− sulfur clusters. One of …

The nitrogen-fixing organism Azotobacter vinelandii contains at least two systems that
catalyze formation of [Fe-S] clusters. One of these systems is encoded by nif genes, whose …

Revised Manuscript Received February 10, 1994• abstract: The nifS gene product (NIFS) is
a pyridoxal phosphate binding enzyme that catalyzes the desulfurization of L-cysteine to …

Among the iron‐sulphur cluster assembly proteins encoded by gene cluster iscSUA‐hscBA‐
fdx in E scherichia coli, IscA has a unique and strong iron binding activity and can provide …

Iron-sulfur clusters are ubiquitous in nature, 1 but the mechanisms for assembly and
insertion of these centers in their cognate proteins are largely unknown. Recent genetic and …

Biogenesis of iron–sulfur clusters requires a concerted delivery of iron and sulfur to target
proteins. It is now clear that sulfur in iron–sulfur clusters is derived from l-cysteine via …