Modulation of ligand–heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond–second temporal range
Author:
Affiliation:
1. Faculty of Life Sciences Manchester Institute of Biotechnology and Photon Science Institute The University of Manchester UK
2. Central Laser Facility Research Complex at Harwell Didcot UK
3. School of Biological Sciences University of Essex UK
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12526
Reference34 articles.
1. Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses
2. How Do Heme-Protein Sensors Exclude Oxygen? Lessons Learned from Cytochrome c′,Nostoc puntiformeHeme Nitric Oxide/Oxygen-Binding Domain, and Soluble Guanylyl Cyclase
3. Mechanism and Biological Role of Nitric Oxide Binding to Cytochrome c‘
4. Regulation and Function of Cytochrome c ′ in Rhodobacter sphaeroides 2.4.3
5. Cytochrome c ′ from Rhodobacter capsulatus Confers Increased Resistance to Nitric Oxide
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