Pub. Date : 1995 Nov 15
PMID : 7492589
1 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | A resonance Raman spectroscopic study of the porcine myoglobin double mutant H64V/V68H has confirmed that the ferric form is bis-histidine ligated, has revealed that the bis-histidine ligation is retained on reduction to the ferrous form, and has demonstrated that CO can displace the ligated distal histidine to produce a ferrous CO form which has a low steady-state photolability, indicating that the replacement histidine blocks the CO escape route from the binding site. | Ferric enterobactin ion | myoglobin | Homo sapiens |