A multiphase Cd-113 NMR investigation of metalloporphyrin reorientation in cadmium-substituted myoglobin

被引：6

作者：

McAteer, K ^{[1
]}

Lipton, AS ^{[1
]}

Kennedy, MA ^{[1
]}

Ellis, PD ^{[1
]}

机构：

[1] ENVIRONM MOL SCI LAB,RICHLAND,WA 99352

来源：

SOLID STATE NUCLEAR MAGNETIC RESONANCE | 1996年 / 7卷 / 03期

关键词：

Cd-113 NMR spectroscopy; ab initio chemical shift calculations; heme isomers; myoglobin;

D O I：

10.1016/S0926-2040(96)01274-X

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Cd-113 NMR spectroscopy in both the solution and solid state has been used to investigate the role of the metal ion and the proximal histidine on metalloporphyrin reorientation in myoglobin. Heme disorder has been known to exist for many years but understanding its mechanism has proved difficult due to the short-lived nature of the minor porphyrin isomer in native myoglobin. Cadmium-substituted myoglobin can be generated in one form which contains different insertion isomers or in another form which contains predominantly only one of these species. This allows for direct investigation of heme disorder in metal-substituted myoglobin.

引用

页码：229 / 238

页数：10

共 30 条

[1]

Ascoli F, 1981, Methods Enzymol, V76, P72

[2]

COLEMAN JE, 1993, METHOD ENZYMOL, V227, P16

[3]

COLLINS DM, 1972, J AM CHEM SOC, V94, P6689, DOI 10.1021/ja00774a021

[4] PROTON NMR-STUDY OF THE INTERACTION OF TIN(IV) PROTOPORPHYRIN-IX MONOMERS AND DIMERS WITH APOMYOGLOBIN [J].