2020
DOI: 10.1021/acs.jpclett.0c02200
|View full text |Cite
|
Sign up to set email alerts
|

Nitrosylation of the Diiron Core Mediated by the N Domain of YtfE

Abstract: The YtfE protein catalyzes the reduction of NO to N2O, protecting iron–sulfur clusters from nitrosylation. The structure of YtfE has a two-domain architecture, with a diiron-containing C-terminal domain linked to an N-terminal domain, in which the function of the latter is enigmatic. Here, by using electron spin resonance (ESR) spectroscopy, we show that YtfE exists in two conformational states, one of which has not been reported. Under high osmotic stress, YtfE adopts a homogeneous conformation (C state) simi… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
12
0

Year Published

2022
2022
2024
2024

Publication Types

Select...
5
1

Relationship

3
3

Authors

Journals

citations
Cited by 6 publications
(12 citation statements)
references
References 16 publications
(24 reference statements)
0
12
0
Order By: Relevance
“…In contrast, E. coli YtfE has been reported to reduce NO to N 2 O in the presence of ascorbate and N , N , N ′, N ′-tetramethyl- p -phenylenediamine (+276 mV), or NADH (−320 mV), albeit rather slowly. 32 , 33 While ascorbate and NADH can clearly act as reductants for YtfE, they are less efficient than DTT ( Figure S3B,C ). Hence, the reduction of YtfE by ascorbate or NADH may be the rate-limiting step in these previously reported assays.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…In contrast, E. coli YtfE has been reported to reduce NO to N 2 O in the presence of ascorbate and N , N , N ′, N ′-tetramethyl- p -phenylenediamine (+276 mV), or NADH (−320 mV), albeit rather slowly. 32 , 33 While ascorbate and NADH can clearly act as reductants for YtfE, they are less efficient than DTT ( Figure S3B,C ). Hence, the reduction of YtfE by ascorbate or NADH may be the rate-limiting step in these previously reported assays.…”
Section: Resultsmentioning
confidence: 99%
“…YtfE is a monomeric L-shaped molecule consisting of two domains (Figure A). The C-terminal hemerythrin-like domain (Pfam: PF01814) contains a nonheme di-iron center. , The globular N-terminal domain (domain of unknown function, DUF542, ScdA_N) contains a pair of highly conserved cysteine residues (Cys30 and Cys31) and caps a long hydrophobic channel, the length of which (∼10–25 Å) is altered by the relative position of ScdA_N to the hemerythrin-like domain. , The thiolates of the cysteine pair are orientated toward this channel and the di-iron site and are prone to oxidation, resulting in a disulfide bond. , A second channel, predominantly hydrophilic in nature, connects the di-iron center to the surrounding solvent. , …”
Section: Introductionmentioning
confidence: 99%
“…EXAFS of E. coli YtfE incubated with NO revealed the formation of a single {FeNO} species, a reaction that yields N 2 O. More recently, the access of NO to the di-iron center of YtfE was proposed to occur through a hydrophobic channel that connects the metal site to the N-terminal domain [31,32]. The ability of YtfE to bind NO is an expected observation as, in general, di-iron proteins bind small molecules like NO, O 2 , azide, thiocyanide, or chloride ions (e.g., [33]).…”
Section: Biochemical and Spectroscopic Properties Of Ricsmentioning
confidence: 99%
“…[19][20][21][22][23][24][25][26][27][28] In this method, nitroxide spin-labels are introduced into the prion molecule, and one can measure the spin-spin interaction between two unpaired electrons at a distance within 20 Å using continuouswave ESR (CW-ESR) and 15 to 60 Å using double electron-electron resonance (DEER) ESR. 13,29,30 To investigate biomolecules with spin-labeled ESR, a nitroxide-based probe is attached through site-directed spin-labeling (SDSL) mutagenesis.…”
Section: Introductionmentioning
confidence: 99%
“…Another physical method, spin‐label electron spin resonance (ESR) spectroscopy, has also been used as a spectroscopic ruler to locate the cross‐β structure in inhomogeneous fibrils or oligomers and to explore the structural conversion and aggregation of proteins or peptides such as amyloid β‐peptides, tau, transthyretin, and prion protein 19–28 . In this method, nitroxide spin‐labels are introduced into the prion molecule, and one can measure the spin–spin interaction between two unpaired electrons at a distance within 20 Å using continuous‐wave ESR (CW‐ESR) and 15 to 60 Å using double electron–electron resonance (DEER) ESR 13,29,30 . To investigate biomolecules with spin‐labeled ESR, a nitroxide‐based probe is attached through site‐directed spin‐labeling (SDSL) mutagenesis.…”
Section: Introductionmentioning
confidence: 99%