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A Nuclear Resonance Vibrational Spectroscopic Study of Oxy Myoglobins Reconstituted with Chemically Modified Heme Cofactors: Insights into the Fe-O2 Bonding and Internal Dynamics of the Protein.

Abstract：

:The molecular mechanism of O2 binding to hemoglobin (Hb) and myoglobin (Mb) is a long-standing issue in the field of bioinorganic and biophysical chemistry. The nature of Fe-O2 bond in oxy Hb and Mb had been extensively investigated by resonance Raman spectroscopy, which assigned the Fe-O2 stretching bands at ∼570 cm-1. However, resonance Raman assignment of the vibrational mode had been elusive due to the spectroscopic selection rule and to the limited information available about the ground-state molecular structure. Thus, nuclear resonance vibrational spectroscopy was applied to oxy Mbs reconstituted with 57Fe-labeled native heme cofactor and two chemically modified ones. This advanced spectroscopy in conjunction with DFT analyses gave new insights into the nature of the Fe-O2 bond of oxy heme by revealing the effect of heme peripheral substitutions on the vibrational dynamics of heme Fe atom, where the main Fe-O2 stretching band of the native protein was characterized at ∼420 cm-1.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Ohta T,Shibata T,Kobayashi Y,Yoda Y,Ogura T,Neya S,Suzuki A,Seto M,Yamamoto Y

doi

10.1021/acs.biochem.8b00829

subject

Has Abstract

pub_date

2018-12-04 00:00:00

pages

6649-6652

issue

48

eissn

0006-2960

issn

1520-4995

journal_volume

57

pub_type

杂志文章

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