Electronic State of the His/Tyr-Ligated Heme of BthA by Mössbauer and DFT Analysis
Author:
Affiliation:
1. Department of Chemistry, Boston University, Boston, Massachusetts 02215, United States
2. Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Inorganic Chemistry,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.inorgchem.0c01349
Reference44 articles.
1. Superfamily of plant, fungal and bacterial peroxidases
2. Heme Enzyme Structure and Function
3. MauG, a Novel Diheme Protein Required for Tryptophan Tryptophylquinone Biogenesis
4. In Crystallo Posttranslational Modification Within a MauG/Pre–Methylamine Dehydrogenase Complex
5. Evidence for Redox Cooperativity between c-Type Hemes of MauG Which Is Likely Coupled to Oxygen Activation during Tryptophan Tryptophylquinone Biosynthesis
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