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The role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis; A NMR study()
Heme oxygenase, HO, cleaves hemin into biliverdin, iron and CO. For mammalian HOs, both native hemin propionates are required for substrate binding and activity. The HO from the pathogenic bacterium Neisseria meningitidis, NmHO, possesses a crystallographically undetected C-terminal fragment that by...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2012
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3514545/ https://ncbi.nlm.nih.gov/pubmed/22913621 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi3007803 |
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