Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins, the nitrophorins
Author:
Affiliation:
1. Max Planck Institute for Chemical Energy Conversion
2. Mülheim an der Ruhr
3. Germany
Abstract
A highly ruffled heme conformation and an extended H-bonding network at the heme active site are the key factors facilitating the unprecedented nitrite dismutase activity of the nitrophorins.
Funder
Max-Planck-Gesellschaft
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2016/SC/C6SC01019A
Reference79 articles.
1. How Biology Handles Nitrite
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4. X-Ray Crystal Structure of a Mutant Assimilatory Nitrite Reductase That Shows Sulfite Reductase-Like Activity
5. Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
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