HOMOTROPIC AND HETEROTROPIC COOPERATIVITY IN THE TETRAHAEM CYTOCHROME C(3) FROM DESULFOVIBRIO-VULGARIS

被引：46

作者：

TURNER, DL

SALGUEIRO, CA

CATARINO, T

LEGALL, J

XAVIER, AV

机构：

[1] UNIV NOVA LISBOA,INST TECNOL QUIM & BIOL,P-2780 OEIRAS,PORTUGAL

[2] UNIV SOUTHAMPTON,DEPT CHEM,SOUTHAMPTON SO9 5NH,HANTS,ENGLAND

[3] UNIV GEORGIA,DEPT BIOCHEM,ATHENS,GA 30602

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 1994年 / 1187卷 / 02期

关键词：

CYTOCHROME C(3); HEME PROTEIN; NMR; 2-DIMENSIONAL; COOPERATIVITY; REDOX-BOHR EFFECT; REDOX MECHANISM;

D O I：

10.1016/0005-2728(94)90117-1

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 thermodynamic parameters which govern the homotropic (e(-)/e(-)) and heterotropic (e(-)/H+) cooperativity in the tetrahaem cytochrome c(3) isolated from Desulfovibrio vulgaris (Hildenborough) were determined, using the paramagnetic shifts of haem methyl groups in the NMR spectra of intermediate oxidized states at different pH levels. A model is put forward to explain how the network of positive and negative cooperativities between the four haems and acid/base group(s) enables the protein to achieve a proton-assisted 2e(-) step.

引用

页码：232 / 235

页数：4

共 14 条

[1] ISOLATION AND CHARACTERIZATION OF FLAVOREDOXIN, A NEW FLAVOPROTEIN THAT PERMITS INVITRO RECONSTITUTION OF AN ELECTRON-TRANSFER CHAIN FROM MOLECULAR-HYDROGEN TO SULFITE REDUCTION IN THE BACTERIUM DESULFOVIBRIO-GIGAS [J].