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

C L  ANDERTON; R E  HESTER; John N. Moore

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

C L ANDERTON, R E HESTER, John N. Moore

Chemistry

Research output: Contribution to journal › Comment/debate › peer-review

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.

Original language	English
Pages (from-to)	1-4
Number of pages	4
Journal	BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Volume	1253
Issue number	1
Publication status	Published - 15 Nov 1995

Keywords

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

Cite this

@article{d91bc26d3e414a95bbc490d80559ba50,

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

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.",

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

author = "ANDERTON, {C L} and HESTER, {R E} and Moore, {John N.}",

year = "1995",

month = nov,

day = "15",

language = "English",

volume = "1253",

pages = "1--4",

journal = "BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY",

issn = "0167-4838",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - RESONANCE RAMAN-SPECTROSCOPY REVEALS NOVEL LIGATION PROPERTIES OF THE PORCINE MYOGLOBIN DOUBLE MUTANT H64V/V68H

AU - ANDERTON, C L

AU - HESTER, R E

AU - Moore, John N.

PY - 1995/11/15

Y1 - 1995/11/15

N2 - 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.

AB - 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.

KW - RESONANCE RAMAN SPECTROSCOPY

KW - LIGATION

KW - DOUBLE MUTANT

KW - MYOGLOBIN (PORCINE)

KW - SITE-DIRECTED MUTAGENESIS

KW - SPERM WHALE MYOGLOBIN

KW - LIGAND-BINDING

KW - CARBON-MONOXIDE

KW - CYTOCHROME

KW - HEME

KW - KINETICS

KW - SPIN

M3 - Comment/debate

SN - 0167-4838

VL - 1253

SP - 1

EP - 4

JO - BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY

JF - BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY

IS - 1

ER -