A new mode for heme-heme interactions in hemoglobin associated with distal perturbations.

Abstract:

:The distal side of the heme pocket, known to regulate ligand affinity, is shown to be directly involved in subunit interactions. Valency hybrids with oxygen or carbon monoxide bound to the reduced chain are used to model R-state hemoglobin with different distal perturbations. Electron paramagnetic resonance of the oxidized chains shows that the carbon monoxide perturbation is transmitted between subunits to the distal histidine and the oxidized iron center. A comparison of hybrids with only one type of chain oxidized and hybrids with a single alpha beta dimer oxidized is consistent with this perturbation being transmitted across the alpha 1 beta 1 interface. This represents a new mode of subunit interactions in hemoglobin.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Levy A,Sharma VS,Zhang L,Rifkind JM

doi

10.1016/S0006-3495(92)81879-9

subject

Has Abstract

pub_date

1992-03-01 00:00:00

pages

750-5

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(92)81879-9

journal_volume

61

pub_type

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