Literature summary for 1.14.14.47 extracted from

Brunel, A.; Wilson, A.; Henry, L.; Dorlet, P.; Santolini, J.
The proximal hydrogen bond network modulates Bacillus subtilis nitric-oxide synthase electronic and structural properties (2011), J. Biol. Chem., 286, 11997-12005.

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Protein Variants

Protein Variants	Comment	Organism
additional information	the proximal hydrogen bond modulation at residue W66 can selectively decrease or increase the electron donating properties of the proximal thiolate. The modulation controls the sigma-competition between distal and proximal ligands and controls the stability of various NOS intermediates. 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	Bacillus subtilis
W66F	mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates	Bacillus subtilis
W66H	mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates	Bacillus subtilis
W66L	mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates	Bacillus subtilis
W66Y	mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O34453	-	-
Bacillus subtilis 168	O34453	-	-

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Release 2023.1 (January 2023)