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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Biophys+Rev
2018 ; 10
(2
): 271-284
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A role of heme side-chains of human hemoglobin in its function revealed by
circular dichroism and resonance Raman spectroscopy
#MMPMID29260461
Nagai M
; Mizusawa N
; Kitagawa T
; Nagatomo S
Biophys Rev
2018[Apr]; 10
(2
): 271-284
PMID29260461
show ga
Structural changes of heme side-chains of human adult hemoglobin (Hb A) upon
ligand (O(2) or CO) dissociation have been studied by circular dichroism (CD) and
resonance Raman (RR) spectroscopies. We point out the occurrence of appreciable
deformation of heme side-chains like vinyl and propionate groups prior to the
out-of-plane displacement of heme iron. Referring to the recent fine resolved
crystal structure of Hb A, the deformations of heme side-chains take place only
in the ? subunits. However, these changes are not observed in the isolated ?
chain (?(4) homotetramer) and, therefore, are associated with the ?-?
inter-subunit interactions. For the communications between ? and ? subunits in Hb
A regarding signals of ligand dissociation, possible routes are proposed on the
basis of the time-resolved absorption, CD, MCD (magnetic CD), and RR
spectroscopies. Our finding of the movements of heme side-chains would serve as
one of the clues to solve the cooperative O(2) binding mechanism of Hb A.