Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins, the nitrophorins
作者： Chunmao He , Hideaki Ogata , Wolfgang Lubitz
DOI: 10.1039/C6SC01019A
关键词:
摘要: Nitrophorins (NPs) catalyze the nitrite dismutation reaction that is unprecedented in ferriheme proteins. Despite progress studying mechanism, fundamental issues regarding correlation of structural features with dismutase activity NPs remain elusive. On other hand, it has been shown complexes are unique among those proteins since some their electron paramagnetic resonance (EPR) spectra show significant highly anisotropic low spin (HALS) signals large gmax values over 3.2. The origin HALS or models not well understood, especially cases where axial ligands than histidine present. In this study several mutations were introduced NP4. related coordination and investigated. As a result, EPR NP–nitrite found to be tightly correlated extent heme ruffling protonation state proximal His ligand—dictated by an extended H-bonding network at active site. Furthermore, established two factors essential determining NPs. These results may provide valuable guide for identifying designing novel similar activity.
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