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Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; Coupling to the distal H-bond network via ordered water molecules
The hydrogen bonding of ligated water in ferric, high-spin, resting-state substrate complexes of heme oxygenase from Neisseria meningitidis has been systematically perturbed by variable electron-withdrawing substituents on the hemin periphery. The pattern of (1)H NMR-detected dipolar shifts due to t...
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| Autori principali: | , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2006
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2566965/ https://ncbi.nlm.nih.gov/pubmed/16683803 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja0578505 |
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