Cloned (Comment) | Organism |
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Bacillus subtilis |
Crystallization (Comment) | Organism |
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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 | UniProt | Comment | Textmining |
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Bacillus subtilis | O34453 | - |
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Bacillus subtilis 168 | O34453 | - |
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