scholarly journals Stepwise Nitrosylation of the Nonheme Iron Site in an Engineered Azurin and a Molecular Basis for Nitric Oxide Signaling Mediated by Nonheme Iron Proteins

2021 ◽  
Author(s):  
Shiliang Tian ◽  
Ruixi Fan ◽  
Therese Albert ◽  
Rahul L. Khade ◽  
Huiguang Dai ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Molecular Basis ◽  
Biological Systems ◽  
Nonheme Iron ◽  
Iron Site ◽  
Iron Species ◽  
Iron Proteins ◽  
Nitric Oxide Signaling ◽  
Dinitrosyl Iron

Mononitrosyl and dinitrosyl iron species, such as {FeNO}7, {FeNO}8 and {Fe(NO)2}9, have been proposed to play pivotal roles in the nitrosylation processes of nonheme iron centers in biological systems. Despite...

scholarly journals Ancient origins of nitric oxide signaling in biological systems

1999 ◽  
Vol 96 (25) ◽  
pp. 14206-14207 ◽  
Author(s):  
J. Durner ◽  
A. J. Gow ◽  
J. S. Stamler ◽  
J. Glazebrook
Keyword(s):  
Nitric Oxide ◽  
Biological Systems ◽  
Nitric Oxide Signaling

scholarly journals Binding of Nitric Oxide in CDGSH-type [2Fe-2S] Clusters of the Human Mitochondrial Protein Miner2

2017 ◽  
Vol 292 (8) ◽  
pp. 3146-3153 ◽  
Author(s):  
Zishuo Cheng ◽  
Aaron P. Landry ◽  
Yiming Wang ◽  
Huangen Ding
Keyword(s):  
Nitric Oxide ◽  
Mitochondrial Protein ◽  
Wolfram Syndrome ◽  
Iron Complex ◽  
Single Mutation ◽  
Subtle Change ◽  
Nitric Oxide Signaling ◽  
Iron Sulfur ◽  
Dinitrosyl Iron ◽  
In Cells

Iron-sulfur proteins are among the primary targets of nitric oxide in cells. Previous studies have shown that iron-sulfur clusters hosted by cysteine residues in proteins are readily disrupted by nitric oxide forming a protein-bound dinitrosyl iron complex, thiolate-bridged di-iron tetranitrosyl complex, or octanitrosyl cluster. Here we report that human mitochondrial protein Miner2 [2Fe-2S] clusters can bind nitric oxide without disruption of the clusters. Miner2 is a member of a new CDGSH iron-sulfur protein family that also includes two mitochondrial proteins: the type II diabetes-related mitoNEET and the Wolfram syndrome 2-linked Miner1. Miner2 contains two CDGSH motifs, and each CDGSH motif hosts a [2Fe-2S] cluster via three cysteine and one histidine residues. Binding of nitric oxide in the reduced Miner2 [2Fe-2S] clusters produces a major absorption peak at 422 nm without releasing iron or sulfide from the clusters. The EPR measurements and mass spectrometry analyses further reveal that nitric oxide binds to the reduced [2Fe-2S] clusters in Miner2, with each cluster binding one nitric oxide. Although the [2Fe-2S] cluster in purified human mitoNEET and Miner1 fails to bind nitric oxide, a single mutation of Asp-96 to Val in mitoNEET or Asp-123 to Val in Miner1 facilitates nitric oxide binding in the [2Fe-2S] cluster, indicating that a subtle change of protein structure may switch mitoNEET and Miner1 to bind nitric oxide. The results suggest that binding of nitric oxide in the CDGSH-type [2Fe-2S] clusters in mitochondrial protein Miner2 may represent a new nitric oxide signaling mode in cells.

Sign in / Sign up

Export Citation Format

Share Document