Confirmation of the assignment of the iron-histidine stretching mode in myoglobin

P. V. Argade, M. Sassaroli, Denis L. Rousseau

Research output: Contribution to journalArticle

99 Citations (Scopus)

Abstract

Resonance Raman spectra of myoglobins reconstituted with hemes isotopically substituted at the central iron atom or the pyrrole nitrogen atoms have been recorded to address the issue of whether the strong line at approximately 220 cm** minus **1 is the iron-histidine stretching mode or the iron-pyrrole nitrogen stretching mode. The frequency of the line at 220 cm** minus **1 is 1. 7 cm** minus **1 lower in myoglobin reconstituted with the **5**7Fe heme than it is in the **5**4Fe-substituted heme. No large shifts were detected in any other Raman lines. When myoglobin reconstituted with **1**5N-substituted pyrrole nitrogens in the heme is compared to the unsubstituted myoglobin no large change is detected in the line at 220 cm** minus **1, but the frequency of the line at 243 cm** minus **1 is 1. 5 cm** minus **1 lower. In comparing myoglobin buffered in D//2O to that buffered in H//2O only the line at 220 cm** minus **1 changes frequency (1. 4 cm** minus **1).

Original languageEnglish (US)
Pages (from-to)6593-6596
Number of pages4
JournalJournal of the American Chemical Society
Volume106
Issue number22
StatePublished - Jan 1 1984
Externally publishedYes

Fingerprint

Myoglobin
Histidine
Stretching
Heme
Iron
Pyrroles
Nitrogen
Atoms
Raman scattering

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Confirmation of the assignment of the iron-histidine stretching mode in myoglobin. / Argade, P. V.; Sassaroli, M.; Rousseau, Denis L.

In: Journal of the American Chemical Society, Vol. 106, No. 22, 01.01.1984, p. 6593-6596.

Research output: Contribution to journalArticle

@article{5a25ab0f623e4a59bf90fea3e303c5b4,
title = "Confirmation of the assignment of the iron-histidine stretching mode in myoglobin",
abstract = "Resonance Raman spectra of myoglobins reconstituted with hemes isotopically substituted at the central iron atom or the pyrrole nitrogen atoms have been recorded to address the issue of whether the strong line at approximately 220 cm** minus **1 is the iron-histidine stretching mode or the iron-pyrrole nitrogen stretching mode. The frequency of the line at 220 cm** minus **1 is 1. 7 cm** minus **1 lower in myoglobin reconstituted with the **5**7Fe heme than it is in the **5**4Fe-substituted heme. No large shifts were detected in any other Raman lines. When myoglobin reconstituted with **1**5N-substituted pyrrole nitrogens in the heme is compared to the unsubstituted myoglobin no large change is detected in the line at 220 cm** minus **1, but the frequency of the line at 243 cm** minus **1 is 1. 5 cm** minus **1 lower. In comparing myoglobin buffered in D//2O to that buffered in H//2O only the line at 220 cm** minus **1 changes frequency (1. 4 cm** minus **1).",
author = "Argade, {P. V.} and M. Sassaroli and Rousseau, {Denis L.}",
year = "1984",
month = "1",
day = "1",
language = "English (US)",
volume = "106",
pages = "6593--6596",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "22",

}

TY - JOUR

T1 - Confirmation of the assignment of the iron-histidine stretching mode in myoglobin

AU - Argade, P. V.

AU - Sassaroli, M.

AU - Rousseau, Denis L.

PY - 1984/1/1

Y1 - 1984/1/1

N2 - Resonance Raman spectra of myoglobins reconstituted with hemes isotopically substituted at the central iron atom or the pyrrole nitrogen atoms have been recorded to address the issue of whether the strong line at approximately 220 cm** minus **1 is the iron-histidine stretching mode or the iron-pyrrole nitrogen stretching mode. The frequency of the line at 220 cm** minus **1 is 1. 7 cm** minus **1 lower in myoglobin reconstituted with the **5**7Fe heme than it is in the **5**4Fe-substituted heme. No large shifts were detected in any other Raman lines. When myoglobin reconstituted with **1**5N-substituted pyrrole nitrogens in the heme is compared to the unsubstituted myoglobin no large change is detected in the line at 220 cm** minus **1, but the frequency of the line at 243 cm** minus **1 is 1. 5 cm** minus **1 lower. In comparing myoglobin buffered in D//2O to that buffered in H//2O only the line at 220 cm** minus **1 changes frequency (1. 4 cm** minus **1).

AB - Resonance Raman spectra of myoglobins reconstituted with hemes isotopically substituted at the central iron atom or the pyrrole nitrogen atoms have been recorded to address the issue of whether the strong line at approximately 220 cm** minus **1 is the iron-histidine stretching mode or the iron-pyrrole nitrogen stretching mode. The frequency of the line at 220 cm** minus **1 is 1. 7 cm** minus **1 lower in myoglobin reconstituted with the **5**7Fe heme than it is in the **5**4Fe-substituted heme. No large shifts were detected in any other Raman lines. When myoglobin reconstituted with **1**5N-substituted pyrrole nitrogens in the heme is compared to the unsubstituted myoglobin no large change is detected in the line at 220 cm** minus **1, but the frequency of the line at 243 cm** minus **1 is 1. 5 cm** minus **1 lower. In comparing myoglobin buffered in D//2O to that buffered in H//2O only the line at 220 cm** minus **1 changes frequency (1. 4 cm** minus **1).

UR - http://www.scopus.com/inward/record.url?scp=0021512620&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021512620&partnerID=8YFLogxK

M3 - Article

VL - 106

SP - 6593

EP - 6596

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 22

ER -