Hydrogen bonding to the bound dioxygen in oxy cobaltous myoglobin reduces the superhyperfine coupling to the proximal histidine
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00147a010
Cited by 21 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Density-functional molecular dynamics studies of biologically relevant iron and cobalt complexes with macrocyclic ligands;Coordination Chemistry Reviews;2008-07
2. Structure and Dynamics of Dioxygen Bound to Cobalt and Iron Heme;Biophysical Journal;2006-09
3. A Superoxo-Ferrous State in a Reduced Oxy-Ferrous Hemoprotein and Model Compounds;Journal of the American Chemical Society;2003-12-01
4. Application of two-dimensional pulsed EPR nutation spectroscopy to a disordered system with largeg-anisotropy;Applied Magnetic Resonance;2003-09
5. Dendritic metalloporphyrins with a distal H-bond donor as mimics of haemoglobinElectronic supplementary information (ESI) available: procedures for the synthesis of 1 and 5 and iron(ii) insertion into the dendritic porphyrins including full spectral characterisation and complete EPR characterisation of the complex 22·Co(dmim) and the corresponding oxygenated complex. See http://www.rsc.org/suppdata/ob/b2/b212468h/;Organic & Biomolecular Chemistry;2003-03-12
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