Exploring the Conformational Variability in the Heme b Propionic Acid Side Chains through the Effect of a Biological Probe: A Study of the Isolated Ions
Author:
Affiliation:
1. Dipartimento di Chimica e Tecnologie del Farmaco, Università degli Studi di Roma La Sapienza, P.le A. Moro 5, I-00185, Roma, Italy
2. Dipartimento di Farmacia, Università G. D’Annunzio, Via dei Vestini 31, I-66100 Chieti, Italy
Funder
European Commission
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp5113476
Reference67 articles.
1. Structural and Functional Aspects of Metal Sites in Biology
2. Role of the Heme Active Site and Protein Environment in Structure, Spectra, and Function of the Cytochrome P450s
3. Heme-Containing Oxygenases
4. Metalloporphyrines as Active Site AnaloguesLessons from Enzymes and Enzyme Models
5. Peptide-Based Heme−Protein Models
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