Effect of solvent viscosity on the heme-pocket dynamics of photolyzed (carbonmonoxy)hemoglobin. - Suppr | 超能文献

Effect of solvent viscosity on the heme-pocket dynamics of photolyzed (carbonmonoxy)hemoglobin.

作者信息

Findsen E W, Friedman J M, Ondrias M R

机构信息

Department of Chemistry, University of New Mexico, Albuquerque 87131.

出版信息

Biochemistry. 1988 Nov 29;27(24):8719-24. doi: 10.1021/bi00424a005.

DOI:10.1021/bi00424a005

Abstract

The heme-pocket dynamics subsequent to carbon monoxide photolysis from human hemoglobin have been monitored as a function of glycerol-water solvent composition with time-resolved resonance Raman spectroscopy. Prompt (geminate) ligand recombination rates and the transient heme-pocket geometry established within 10 ns after photolysis appear to be largely independent of solvent composition. The rate of relaxation of the transient geometry to an equilibrium deoxy configuration is, however, quite sensitive to solvent composition. These observations suggest that the former processes result from local, internal motions of the protein, while the relaxation dynamics of the proximal heme pocket are predicated upon more global protein motions that are dependent upon solvent viscosity.

摘要

相似文献

1

Effect of solvent viscosity on the heme-pocket dynamics of photolyzed (carbonmonoxy)hemoglobin.

Biochemistry. 1988 Nov 29;27(24):8719-24. doi: 10.1021/bi00424a005.

2

Heme-CO religation in photolyzed hemoglobin: a time-resolved Raman study of the Fe-CO stretching mode.

Biochemistry. 1993 Feb 9;32(5):1318-23. doi: 10.1021/bi00056a017.

3

Response of the local heme environment of (carbonmonoxy)hemoglobin to protein dehydration.

Biochemistry. 1986 Dec 2;25(24):7912-7. doi: 10.1021/bi00372a019.

4

Time-resolved Raman spectroscopy with subpicosecond resolution: vibrational cooling and delocalization of strain energy in photodissociated (carbonmonoxy)hemoglobin.

Biochemistry. 1987 Dec 1;26(24):7914-23. doi: 10.1021/bi00398a056.

5

Ligand binding to heme proteins: connection between dynamics and function.

Biochemistry. 1991 Apr 23;30(16):3988-4001. doi: 10.1021/bi00230a026.

6

Nanosecond step-scan FTIR spectroscopy of hemoglobin: ligand recombination and protein conformational changes.

Biochemistry. 1996 Oct 8;35(40):13001-5. doi: 10.1021/bi961522n.

7

Kinetic modulation in carbonmonoxy derivatives of truncated hemoglobins: the role of distal heme pocket residues and extended apolar tunnel.

J Biol Chem. 2003 Jul 18;278(29):27241-50. doi: 10.1074/jbc.M212634200. Epub 2003 May 7.

8

Hydrophobic distal pocket affects NO-heme geminate recombination dynamics in dehaloperoxidase and H64V myoglobin.

J Phys Chem B. 2006 Jul 27;110(29):14483-93. doi: 10.1021/jp056790m.

9

Evidence for sub-picosecond heme doming in hemoglobin and myoglobin: a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species.

Biochemistry. 1995 Jan 31;34(4):1224-37. doi: 10.1021/bi00004a016.

10

Transient Raman study of horseradish peroxidase. Evidence for a lack of extensive heme pocket relaxation subsequent to carbon monoxide photolysis.

J Biol Chem. 1985 Oct 5;260(22):12194-7.

引用本文的文献

1

The effect of water on the rate of conformational change in protein allostery.

Biophys J. 2001 Nov;81(5):2919-34. doi: 10.1016/S0006-3495(01)75932-2.

文献AI研究员

20分钟写一篇综述，助力文献阅读效率提升50倍。

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

文档翻译

学术文献翻译模型，支持多种主流文档格式。