STRUCTURE OF THE HEME O PROSTHETIC GROUP FROM THE TERMINAL QUINOL OXIDASE OF ESCHERICHIA-COLI

被引：68

作者：

WU, W

CHANG, CK

VAROTSIS, C

BABCOCK, GT

PUUSTINEN, A

WIKSTROM, M

机构：

[1] MICHIGAN STATE UNIV,DEPT CHEM,E LANSING,MI 48824

[2] UNIV HELSINKI,DEPT MED CHEM,HELSINKI BIOENERGET GRP,SF-00170 HELSINKI 17,FINLAND

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 1992年 / 114卷 / 04期

关键词：

D O I：

10.1021/ja00030a009

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The structure of the heme o prosthetic group of Escherichia coli quinol oxidase (cytochrome o oxidase) has been unambiguously determined by preparation and characterization of its iron-free derivative porphyrin o dimethyl ester, or dimethyl 2,7,12,18-tetramethyl-3-[(4E,8E)-1-hydroxy-5,9,13-trimethyltetradeca-4,8,12-trienyl]-8-vinylporphine-13,17-dipropionate. The identity of this natural porphyrin dimethyl ester was established by H-1 NMR, MS, IR, and RR spectroscopies as well as by comparisons with model compounds and the closely related porphyrin a dimethyl ester. The reliability of the structure determination was further strengthened by the isolation and characterization of the acetylated and dehydrated derivatives of porphyrin o.

引用

页码：1182 / 1187

页数：6

共 31 条

[1] RESONANCE RAMAN-SPECTRA OF OCTAETHYLPORPHYRINATO-NI(II) AND MESO-DEUTERATED AND N-15 SUBSTITUTED DERIVATIVES .2. NORMAL COORDINATE ANALYSIS [J].