High pressure reveals structural determinants for globin hexacoordination: Neuroglobin and myoglobin cases

被引：41

作者：

Capece, L. ^{[1
]}

Marti, M. A. ^{[1
]}

Bidon-Chanal, A. ^{[2
,3
]}

Nadra, A. ^{[1
]}

Luque, E. J. ^{[2
,3
]}

Estrin, D. A. ^{[1
]}

机构：

[1] Univ Buenos Aires, Fac Ciencias Exactas & Nat, CONICET, INQUIMAE,Dept Quim Inorgan Analit & Quim Fis, Buenos Aires, DF, Argentina

[2] Univ Barcelona, Fac Farm, Dept Fisicoquim, E-08028 Barcelona, Spain

[3] Univ Barcelona, Fac Farm, Inst Biomed IBUB, E-08028 Barcelona, Spain

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2009年 / 75卷 / 04期

关键词：

molecular dynamics; globins hexacoordination; essential dynamics; MOLECULAR-DYNAMICS SIMULATION; HYDROPHOBIC INTERACTIONS; PROTEIN-STRUCTURE; HEME-PROTEINS; HEMOGLOBIN; LIGAND; AFFINITY; NO; RECOGNITION; CYTOGLOBIN;

D O I：

10.1002/prot.22297

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The influence of pressure on the equilibrium between five-(5c) and six-coordination (6c) forms in neuroglobin (Ngb) and myoglobin (Mb) has been examined by means of molecular dynamics (MD) simulations at normal and high pressure. The results show that the main effect of high pressure is to reduce the protein mobility without altering the structure in a significant manner. Moreover, our data suggest that the equilibrium between 5c and 6c states in globins is largely controlled by the structure and dynamics of the C-D region. Finally, in agreement with the available experimental data, the free energy profiles obtained from steered MD for both proteins indicate that high pressure enhances hexacoordination. in Ngb, the shift in equilibrium is mainly related to an increase in the 6c -> 5c transition barrier, whereas in Mb such a shift is primarily due to a destabilization of the 5c state.

引用

页码：885 / 894

页数：10

共 45 条

[1] ESSENTIAL DYNAMICS OF PROTEINS [J].