Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Analysis of Fluctuation in the Heme-Binding Pocket and Heme Distortion in Hemoglobin and Myoglobin

Version 1 : Received: 28 December 2021 / Approved: 29 December 2021 / Online: 29 December 2021 (23:52:57 CET)

A peer-reviewed article of this Preprint also exists.

Kondo, H.X.; Takano, Y. Analysis of Fluctuation in the Heme-Binding Pocket and Heme Distortion in Hemoglobin and Myoglobin. Life 2022, 12, 210. Kondo, H.X.; Takano, Y. Analysis of Fluctuation in the Heme-Binding Pocket and Heme Distortion in Hemoglobin and Myoglobin. Life 2022, 12, 210.

Abstract

Heme is located in the active site of proteins and has diverse and important biological functions, such as electron transfer and oxygen transport and/or storage. The distortion of heme porphyrin is considered an important factor for the diverse functions of heme because it correlates with the physical properties of heme, such as oxygen affinity and redox potential. Therefore, clarification of the relationship between heme distortion and the protein environment is crucial in protein science. Here, we analyzed the fluctuation in heme distortion in the protein environment for hemoglobin and myoglobin using molecular dynamics (MD) simulations and quantum mechanical (QM) calculations. We also investigated the protein structures of hemoglobin and myoglobin stored in Protein Data Bank and found that heme is distorted along the doming mode, which correlates with its oxygen affinity, more prominently in the protein environment than in the isolated state, and the magnitude of distortion is different between hemoglobin and myoglobin. This tendency was also observed in the results of MD simulations and QM calculations. These results suggest that heme distortion is affected by its protein environment and fluctuates around its fitted conformation, leading to physical properties that are appropriate for protein functions.

Keywords

heme distortion; pocket rigidity; protein environment; hemoglobin; myoglobin; MD simulation; ONIOM

Subject

Biology and Life Sciences, Biochemistry and Molecular Biology

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