CONTROL AND RECOGNITION OF ANIONIC LIGANDS IN MYOGLOBIN

被引：38

作者：

CUTRUZZOLA, F

ALLOCATELLI, CT

ASCENZI, P

BOLOGNESI, M

SLIGAR, SG

BRUNORI, M

机构：

[1] UNIV ROME LA SAPIENZA,CNR,CTR MOLEC BIOL,I-00185 ROME,ITALY

[2] UNIV PAVIA,DEPT GENET & MICROBIOL,CRYSTALLOG SECT,I-27100 PAVIA,ITALY

[3] UNIV ILLINOIS,ROGER ADAMS LAB,DEPT CHEM & BIOCHEM,URBANA,IL 61801

来源：

FEBS LETTERS | 1991年 / 282卷 / 02期

关键词：

PROTEIN ENGINEERING; MYOGLOBIN MUTANT; LIGAND BINDING;

D O I：

10.1016/0014-5793(91)80495-O

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：

Equilibrium and kinetic experiments on site-directed mutants of a synthetic sperm whale myoglobin (Mb) gene have been performed. Results on the reactivity on both ferric and ferrous wild type and mutants Mb's are presented. Analysis of ligand binding to His(E7)Val and His(E7)Val-Thr(E10)Arg mutants compared to wild-type sperm whale, horse and Aplysia limacina Mb's, shows that the introduction of an arginyl residue at the topological position E10 greatly enhances the stability of the various Mb:heme ligand adducts. Alternative mechanisms of ligand stabilization may therefore be operative in Mb's lacking the distal histidine.

引用

页码：281 / 284

页数：4

共 19 条

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ANTONINI E, 1971, HEMOGLOBIN MYOGLOBIN

[2] APLYSIA-LIMACINA MYOGLOBIN - CRYSTALLOGRAPHIC ANALYSIS AT 1.6-A RESOLUTION [J].