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RESONANCE RAMAN-SPECTROSCOPY REVEALS NOVEL LIGATION PROPERTIES OF THE PORCINE MYOGLOBIN DOUBLE MUTANT H64V/V68H

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Publication details

JournalBIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
DatePublished - 15 Nov 1995
Issue number1
Volume1253
Number of pages4
Pages (from-to)1-4
Original languageEnglish

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.

    Research areas

  • RESONANCE RAMAN SPECTROSCOPY, LIGATION, DOUBLE MUTANT, MYOGLOBIN (PORCINE), SITE-DIRECTED MUTAGENESIS, SPERM WHALE MYOGLOBIN, LIGAND-BINDING, CARBON-MONOXIDE, CYTOCHROME, HEME, KINETICS, SPIN

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