Literature summary for 1.14.14.47 extracted from

Pant, K.; Crane, B.R.
Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation (2006), Biochemistry, 45, 2537-2544.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of the Fe(III)-NO complex with Nomega-hydroxy-L-arginine show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound Nomega-hydroxy-L-arginine. In the Fe(II)-NO complexes, the protonated Nomega-hydroxy-L-arginine Nomega atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. The L-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen	Bacillus subtilis

Crystallization (Comment)

Organism

structures of the Fe(III)-NO complex with Nomega-hydroxy-L-arginine show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound Nomega-hydroxy-L-arginine. In the Fe(II)-NO complexes, the protonated Nomega-hydroxy-L-arginine Nomega atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. The L-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen

Bacillus subtilis

Organism

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

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Release 2023.1 (January 2023)