2021
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Abstract: In heme proteins, the canonical and reversed conformations result from the rotation of the heme group by 180 about the α,γ-meso axis in the protein pocket. The coexistence of the two different heme orientations has been observed both in proteins reconstituted with hemin and in some native proteins. The reversal of the heme orientation can also change certain functional properties of heme proteins. Complementing the results from other experimental techniques, like circular dichroism and nuclear magnetic resonan… Show more

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“…The increase of the canonical heme insertion with respect to the reversed form tends to be a common feature in CDloop-altered mutants (Supporting Information Figure S4). RR does not give any clear evidence of the presence of two protein conformations corresponding to MON 1 and MON 2 found in the crystal. However, in the 1450–1550 cm –1 region, where only the ν 3 core size marker band is expected, the solution spectrum of the CDless mutant cannot be fitted like it has been done for Ngb wild-type and other mutants (two bands at 1500.5 and 1506.5 cm –1 , Supporting Information Figure S5).…”
Section: Resultssupporting
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rupbmjkragerfmgwileyiopcupepmcmbcthiemesagefrontiersapsiucrarxivemeralduhksmucshluniversity-of-gavle
“…The increase of the canonical heme insertion with respect to the reversed form tends to be a common feature in CDloop-altered mutants (Supporting Information Figure S4). RR does not give any clear evidence of the presence of two protein conformations corresponding to MON 1 and MON 2 found in the crystal. However, in the 1450–1550 cm –1 region, where only the ν 3 core size marker band is expected, the solution spectrum of the CDless mutant cannot be fitted like it has been done for Ngb wild-type and other mutants (two bands at 1500.5 and 1506.5 cm –1 , Supporting Information Figure S5).…”
Section: Resultssupporting
“…Another remarkable feature, so far only described in murine Ngb, is the almost random heme insertion: the heme has been observed in reversed and canonical orientations compared to the Mb structure, in a 70:30 proportion, due to the loose heme contacts necessary to allow heme sliding. 9 , 16 19 …”
Section: Introductionmentioning
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“…The reversal of the heme orientation can also change certain functional properties of heme proteins. Sebastiani et al ( Detecting rotational disorder in heme proteins: A comparison between resonance Raman spectroscopy, nuclear magnetic resonance, and circular dichroism , Universita di Firenze, Italy) [ 44 ] compare resonance Raman spectroscopy, nuclear magnetic resonance, and circular dichroism. Raman spectroscopy provides detailed information on the structure of the reversed heme.…”
Section: Biological Compoundsmentioning