2004
DOI: 10.1021/bi048811t
|View full text |Cite
|
Sign up to set email alerts
|

Properties of the Cysteine Residues and Iron−Sulfur Cluster of the Assimilatory 5‘-Adenylyl Sulfate Reductase from Pseudomonas aeruginosa

Abstract: APS reductase from Pseudomonas aeruginosa has been shown to contain a [4Fe-4S] cluster. Thiol determinations and site-directed mutagenesis studies indicate that the single [4Fe-4S] cluster contains only three cysteine ligands, instead of the more typical arrangement in which clusters are bound to the protein by four cysteines. Resonance Raman studies in the Fe-S stretching region are also consistent with the presence of a redox-inert [4Fe-4S](2+) cluster with three cysteinate ligands and indicate that the four… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

8
67
0

Year Published

2005
2005
2015
2015

Publication Types

Select...
5
1
1

Relationship

1
6

Authors

Journals

citations
Cited by 35 publications
(75 citation statements)
references
References 30 publications
(56 reference statements)
8
67
0
Order By: Relevance
“…Notably, a gene encoding an ortholog of CysC (an APS kinase producing 3Ј phosphoadenosine 5Ј phosphosulfate from APS) is absent from this gene cluster. However, there is an ORF encoding a putative ortholog of bacterial "CysH"-type reductases that utilizes APS as a substrate (1,5,26,28). The cluster also encodes a putative sulfite reductase component (CysI), which is similar (43%) to the hemoprotein subunit of E. coli sulfite reductase and 78% similar to that of P. aeruginosa (21), and a putative ortholog of uroporphyrinogen III methylase (CysG), an enzyme involved in synthesis of the siroheme cofactor of sulfite reductase (60).…”
Section: Discussionmentioning
confidence: 99%
“…Notably, a gene encoding an ortholog of CysC (an APS kinase producing 3Ј phosphoadenosine 5Ј phosphosulfate from APS) is absent from this gene cluster. However, there is an ORF encoding a putative ortholog of bacterial "CysH"-type reductases that utilizes APS as a substrate (1,5,26,28). The cluster also encodes a putative sulfite reductase component (CysI), which is similar (43%) to the hemoprotein subunit of E. coli sulfite reductase and 78% similar to that of P. aeruginosa (21), and a putative ortholog of uroporphyrinogen III methylase (CysG), an enzyme involved in synthesis of the siroheme cofactor of sulfite reductase (60).…”
Section: Discussionmentioning
confidence: 99%
“…2ϩ cluster in PaAPR is partially converted to the [3Fe-4S] ϩ form by treatment with the oxidant potassium ferricyanide (16). To assess this possibility for MtAPR, a stoichiometric amount of potassium ferricyanide was added to the enzyme.…”
Section: Ferricyanide Oxidation Of the [4fe-4s] 2ϩ Cluster In Mtapr-mentioning
confidence: 99%
“…Other interactions with the iron-sulfur cluster involve Thr-87 and Trp-246. In the active site, the phosphosulfate group of APS is positioned opposite the [4Fe-4S] cluster, and although no atoms intervene, the sulfate moiety is not in direct contact with the [4Fe-4S] cluster.Given the unusual Cys-Cys dyad coordination and its requirement for catalytic activity, defining the function and properties of the iron-sulfur cluster in APR has generated considerable interest (1,5,7,16,17). Most proteins containing [4Fe-4S] clusters are redox-active (18 -21); however, the [4Fe-4S] 2ϩ cluster in APR does not undergo redox changes during the catalytic cycle (1).…”
mentioning
confidence: 99%
See 2 more Smart Citations