Source:http://linkedlifedata.com/resource/pubmed/id/21310962
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
14
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| pubmed:dateCreated |
2011-4-4
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| pubmed:abstractText |
Bacterial nitric-oxide synthase (NOS)-like proteins are believed to be genuine NOSs. As for cytochromes P450 (CYPs), NOS-proximal ligand is a thiolate that exerts a push effect crucial for the process of dioxygen activation. Unlike CYPs, this catalytic electron donation seems controlled by a hydrogen bond (H-bond) interaction between the thiolate ligand and a vicinal tryptophan. Variations of the strength of this H-bond could provide a direct way to tune the stability along with the electronic and structural properties of NOS. We generated five different mutations of bsNOS Trp66, which can modulate this proximal H-bond. We investigated the effects of these mutations on different NOS complexes (FeIII, FeIICO, and FeIINO), using a combination of UV-visible absorption, EPR, FTIR, and resonance Raman spectroscopies. Our results indicate that (i) the proximal H-bond modulation can selectively decrease or increase the electron donating properties of the proximal thiolate, (ii) this modulation controls the ?-competition between distal and proximal ligands, (iii) this H-bond controls the stability of various NOS intermediates, and (iv) a fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
1083-351X
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
8
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| pubmed:volume |
286
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
11997-2005
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| pubmed:meshHeading |
pubmed-meshheading:21310962-Bacillus subtilis,
pubmed-meshheading:21310962-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:21310962-Hydrogen Bonding,
pubmed-meshheading:21310962-Nitric Oxide Synthase,
pubmed-meshheading:21310962-Oxidative Stress,
pubmed-meshheading:21310962-Protein Structure, Secondary,
pubmed-meshheading:21310962-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:21310962-Spectrum Analysis, Raman
|
| pubmed:year |
2011
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| pubmed:articleTitle |
The proximal hydrogen bond network modulates Bacillus subtilis nitric-oxide synthase electronic and structural properties.
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| pubmed:affiliation |
Commissariat à l'Energie Atomique, iBiTec-S, SBSM, F-91191 Gif-sur-Yvette, France.
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| pubmed:publicationType |
Journal Article
|