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. 1995 Nov 15;1253(1):1-4.
doi: 10.1016/0167-4838(95)00177-v.

Resonance Raman spectroscopy reveals novel ligation properties of the porcine myoglobin double mutant H64V/V68H

C L Anderton  1 , R E Hester, J N Moore
Affiliations

Resonance Raman spectroscopy reveals novel ligation properties of the porcine myoglobin double mutant H64V/V68H

C L Anderton et al. Biochim Biophys Acta. .

Abstract

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.

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