Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation

被引：318

作者：

Barends, Thomas R. M. ^{[1
]}

Foucar, Lutz ^{[1
]}

Ardevol, Albert ^{[2
]}

Nass, Karol ^{[1
]}

Aquila, Andrew ^{[3
]}

Botha, Sabine ^{[1
]}

Doak, R. Bruce ^{[1
]}

Falahati, Konstantin ^{[4
]}

Hartmann, Elisabeth ^{[1
]}

Hilpert, Mario ^{[1
]}

Heinz, Marcel ^{[2
,4
]}

Hoffmann, Matthias C. ^{[5
]}

Koefinger, Juergen ^{[2
]}

Koglin, Jason E. ^{[5
]}

Kovacsova, Gabriela ^{[1
]}

Liang, Mengning ^{[5
]}

Milathianaki, Despina ^{[5
]}

Lemke, Henrik T. ^{[5
]}

Reinstein, Jochen ^{[1
]}

Roome, Christopher M. ^{[1
]}

Shoeman, Robert L. ^{[1
]}

Williams, Garth J. ^{[5
]}

Burghardt, Irene ^{[4
]}

Hummer, Gerhard ^{[2
]}

Boutet, Sebastien ^{[5
]}

Schlichting, Ilme ^{[1
]}

机构：

[1] Max Planck Inst Med Res, D-69120 Heidelberg, Germany

[2] Max Planck Inst Biophys, D-60438 Frankfurt, Germany

[3] European XFEL GmbH, D-22761 Hamburg, Germany

[4] Goethe Univ Frankfurt, Inst Phys & Theoret Chem, D-60438 Frankfurt, Germany

[5] SLAC Natl Accelerator Lab, LCLS, Menlo Pk, CA 94025 USA

来源：

SCIENCE | 2015年 / 350卷 / 6259期

关键词：

FREE-ELECTRON LASER; MOLECULAR-DYNAMICS SIMULATION; NORMAL MODE ANALYSIS; HEME-PROTEINS; CARBONMONOXY MYOGLOBIN; STRUCTURAL DYNAMICS; HEMOGLOBIN; CRYSTALLOGRAPHY; RELAXATION; RESOLUTION;

D O I：

10.1126/science.aac5492

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 femtoseconds, with the C, F, and H helices moving away from the heme cofactor and the E and A helices moving toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, our calculations support the prediction that an immediate collective response of the protein occurs upon ligand dissociation, as a result of heme vibrational modes coupling to global modes of the protein.

引用

页码：445 / 450

页数：6

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