Spectroelectrochemical Investigation of Intramolecular and Interfacial Electron-Transfer Rates Reveals Differences Between Nitrite Reductase at Rest and During Turnover
Author:
Affiliation:
1. Leiden Institute of Physics, Leiden University, P.O. Box 9504, 2300 RA, Leiden, The Netherlands
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja204891v
Reference52 articles.
1. Adman, E. T.; Murphy, M. E. P.Handbook of Metalloproteins;Messerschmidt, A., Huber, R., Wieghardt, K., Poulos, T., Eds.John Wiley & Sons, Ltd.,Chichester, U.K., 2001, 1381.
2. X-ray Structure and Site-Directed Mutagenesis of a Nitrite Reductase from Alcaligenes Faecalis S-6: Roles of Two Copper Atoms in Nitrite Reduction
3. Evidence that the Type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase
4. Studies on Protein-Protein Interaction between Copper-containing Nitrite Reductase and Pseudoazurin from Alcaligenes faecalis S-6
5. A Blue Protein as an Inactivating Factor for Nitrite Reductase from Alcaligenes faecalis Strain S-6
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