A chemometric analysis of the resonance Raman spectra of mutant carbonmonoxy-myoglobins reveals the effects of polarity (Q73164749)

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1 November 2019

title

A chemometric analysis of the resonance Raman spectra of mutant carbonmonoxy-myoglobins reveals the effects of polarity (English)

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1 November 2019

author name string

C L Anderton

series ordinal

1

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1 November 2019

R E Hester

series ordinal

2

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1 November 2019

J N Moore

series ordinal

3

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1 November 2019

language of work or name

English

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publication date

1 March 1997

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Biochimica et Biophysica Acta

1 November 2019

published in

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1 November 2019

volume

1338

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1 November 2019

issue

1

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1 November 2019

page(s)

107-120

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Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change

1 November 2019

cites work

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X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution

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Rebinding and relaxation in the myoglobin pocket

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High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin

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Structural determinants of the stretching frequency of CO bound to myoglobin

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Distal pocket polarity in ligand binding to myoglobin: deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by X-ray crystallography and infrared spectroscopy

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7 January 2021

The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers

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Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O

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Resonance Raman spectroscopic studies of ligated mutant myoglobins.

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Identification of the iron-carbonyl stretch in distal histidine mutants of carbonmonoxymyoglobin.

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Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes

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Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: detection of Fe(III)--NO stretching, Fe(III)--N--O bending, and Fe(II)--N--O bending vibrations

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Resonance raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement.

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Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin

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Time-resolved resonance Raman study on the binding of carbon monoxide to recombinant human myoglobin and its distal histidine mutants

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Distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of three distal mutants

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Structural and functional effects of apolar mutations of the distal valine in myoglobin

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Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin

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Distal pocket polarity in ligand binding to myoglobin: structural and functional characterization of a threonine68(E11) mutant

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Structure of myoglobin-ethyl isocyanide histidine as a swinging door for ligand entry

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Is bound carbonyl linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data

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7 January 2021

10.1016/S0167-4838(96)00194-X

Identifiers

DOI

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1 November 2019

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