The Dynamics Behind the Affinity: Controlling Heme-Gas Affinity via Geminate Recombination and Heme Propionate Conformation in the NO Carrier Cytochrome c′-Reference-Cited by-同舟云学术

The Dynamics Behind the Affinity: Controlling Heme-Gas Affinity via Geminate Recombination and Heme Propionate Conformation in the NO Carrier Cytochrome c′

Published:2016-10-12 Issue:11 Volume:11 Page:3191-3201
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Andrew Colin R.¹,Petrova Olga N.²,Lamarre Isabelle²,Lambry Jean-Christophe²,Rappaport Fabrice³,Negrerie Michel²

Affiliation:

1. Department of Chemistry and Biochemistry, Eastern Oregon University, La Grande, Oregon 97850, United States

2. Laboratoire d’Optique et Biosciences, INSERM, Ecole Polytechnique, 91128 Palaiseau, France

3. Laboratoire de Physiologie Membranaire et Moléculaire du Chloroplaste, CNRS, Université Pierre et Marie Curie, 75005 Paris, France

Funder

Division of Molecular and Cellular Biosciences

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.6b00599

Reference58 articles.

1. A “Sliding Scale Rule” for Selectivity among NO, CO, and O2 by Heme Protein Sensors

2. Spin-dependent mechanism for diatomic ligand binding to heme

3. Temperature-Dependent Studies of NO Recombination to Heme and Heme Proteins

4. Temperature-dependent heme kinetics with nonexponential binding and barrier relaxation in the absence of protein conformational substates

5. Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins

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